Escherichia coli K-12 substr. MG1655 Polypeptide: protein chain initiation factor IF2

Gene: infB Accession Numbers: EG10505 (EcoCyc), b3168, ECK3157

Synonyms: ssyG, IF-2

Regulation Summary Diagram: ?

Regulation summary diagram for infB

IF2 is one of three translation initiation factors in E. coli [Dubnoff69, Revel68, Iwasaki68]; together with IF1, it ensures the correct binding of fMet-tRNAfMet in the ribosomal P site [Lockwood71, Antoun06].

Kinetic data show that IF2 is the primary factor responsible for recognition of the formyl group of fMet-tRNAfMet [Majumdar76, Sundari76, Antoun06]. IF2 interacts with the 30S ribosomal subunit at two distinct sites [Caserta06]. IF2 interacts with the C-terminal domain of 50S ribosomal subunit protein L7/L12 dimer [Fakunding73, Helgstrand07]; the interaction is important for IF2-mediated subunit association [Mandava12]. IF2 stimulates ternary complex formation of leaderless mRNAs with the 30S subunit [Grill00, Grill01] and is required for efficient translation reinitiation at the downstream open reading frame in a translationally coupled operon [Yoo08].

IF2 has ribosome-dependent GTPase activity [Kolakofsky68, Dubnoff72] with approximately 10 times higher affinity for GDP than for GTP [Pon85]. Domain IV of IF2 is the GTP-binding domain. Mutations in several amino acid residues in the GTP-binding domain render IF2 nonfunctional or cold-sensitive, suggesting that GTP hydrolysis is important for IF2 function [Laalami94, Laursen03]. GTP hydrolysis occurs during the formation of the 70S initiation complex [Luchin99, Tomsic00] and has been implicated in release of IF2 from the 70S ribosome [Lelong70, Lockwood72, Luchin99, Antoun03]. GTP-bound IF2 is required for mRNA restructuring during formation of the 30S preinitiation complex [Studer06]. The alarmone ppGpp can bind to IF2 at the same site as GTP and interferes with translation initiation [Milon06].

IF2 exists in three isoforms, IF2α (IF2-1), IF2β (IF2-2), and IF2β' (IF2γ, IF2-3) [Miller73a, Nyengaard91, MorelDeville90, Plumbridge85, Sacerdot92], which are generated by the use of alternative in-frame translation initiation codons: IF2α is the full-length protein, GUG at position 158 is used as the initiation codon for IF2β, and AUG at position 165 is used for IF2β' [Mortensen95]. Both the α and β forms are required for optimal growth; the isoforms thus have acquired specialized, although not essential functions [Sacerdot92]. IF2β was identified as the host factor MRFα-PR required for phage Mu replication [North07].

The N-terminal region of IF2 is required for optimal interaction with the 30S and 50S ribosomal subunits [Moreno99]. A solution structure of the N-terminal domain I of IF2 (IF2N) has been solved [Laursen03a]. A flexible linker region connects this domain to the conserved C-terminal domains of IF2 [Laursen04]. A cryo-EM reconstruction of the initiation complex shows a conformation of IF2 that is different from that seen in the crystal structure of the Methanobacterium thermoautotrophicum protein aIF5B [Allen05]. The solution structure of the four C-terminal domains of IF2 also shows structural differences between IF2 and aIF5B [Rasmussen08]. Addition of GDP or a non-hydrolyzable analog of GTP causes a structural transition [Vohlander11]. Cryo-EM reconstruction of the 30S translation initiation complex shows that IF2 contacts the 16S rRNA, IF1, and S12 [Julian11]. IF2 and EF-G appear to compete for the same binding site on the ribosome [Cameron02].

IF2 was shown to have chaperone-like function [Caldas00]; interestingly, IF2 levels are increased under osmotic stress conditions [Weber06].

infB is an essential gene [Laalami91]. The ssyG class of cold-sensitive mutations localizes to infB [Shiba86]. Several infB mutations result in cold-sensitive growth, including mutations in the GTP-binding domain [Laursen03]. The gicD1 allele, resulting in a V697I substitution in IF2, confers cold sensitive growth and suppresses rpsL31-mediated streptomycin resistance at 15°C [Rath09].

Reviews: [Laalami91a, Schmitt96, Rodnina00, Caldon01, Boelens02, Moll02, Laursen05, Mechulam11]

Citations: [Milon07, Burakovskii07, Qin09, Mazumder72, Benne73, Fakunding73a, Krauss75, Naaktgeboren75, Hamel75, vanderHofstad76, Heimark76, Berthelot77, vanderHofstad78, Beaudry79, Petersen79, vanderLaken80, Travers80, Schmitt80, Weiel82, Plumbridge82, Wintermeyer83, Boileau83, Plumbridge83, Sacerdot84, Canonaco86, Cenatiempo87, Cole87a, Hartz89, Wakao89, Romby90, Wakao90, Vachon90, Wakao91, La93, Mangroo95, Yusupova96, Wu97, Steffensen97, Karimi98, Moreno98, Thanedar00, Guillon96, Larigauderie00, La01, Mayer03, Brandi04]

Gene Citations: [Sands88, Nakamura85, Neidhardt96, Regnier89, Regnier90]

Locations: cytosol, membrane

Map Position: [3,311,364 <- 3,314,036] (71.37 centisomes, 257°)
Length: 2673 bp / 890 aa

Molecular Weight of Polypeptide: 97.35 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0010410 , CGSC:597 , DIP:DIP-36182N , EchoBASE:EB0500 , EcoGene:EG10505 , EcoliWiki:b3168 , Mint:MINT-1235405 , ModBase:P0A705 , OU-Microarray:b3168 , PortEco:infB , PR:PRO_000023013 , Pride:P0A705 , Protein Model Portal:P0A705 , RefSeq:NP_417637 , RegulonDB:EG10505 , SMR:P0A705 , UniProt:P0A705

Relationship Links: InterPro:IN-FAMILY:IPR000178 , InterPro:IN-FAMILY:IPR000795 , InterPro:IN-FAMILY:IPR004161 , InterPro:IN-FAMILY:IPR005225 , InterPro:IN-FAMILY:IPR006847 , InterPro:IN-FAMILY:IPR009000 , InterPro:IN-FAMILY:IPR009061 , InterPro:IN-FAMILY:IPR013575 , InterPro:IN-FAMILY:IPR015760 , InterPro:IN-FAMILY:IPR023115 , InterPro:IN-FAMILY:IPR027417 , Panther:IN-FAMILY:PTHR23115:SF41 , PDB:Structure:1ND9 , PDB:Structure:1ZO1 , Pfam:IN-FAMILY:PF00009 , Pfam:IN-FAMILY:PF03144 , Pfam:IN-FAMILY:PF04760 , Pfam:IN-FAMILY:PF08364 , Pfam:IN-FAMILY:PF11987 , Prosite:IN-FAMILY:PS01176 , Prosite:IN-FAMILY:PS51722

In Paralogous Gene Group: 77 (16 members) , 321 (6 members)

Genetic Regulation Schematic: ?

Genetic regulation schematic for infB

GO Terms:

Biological Process: GO:0006413 - translational initiation Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Lockwood71]
GO:0006412 - translation Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0003743 - translation initiation factor activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Lockwood71, Iwasaki68, Revel68, Plumbridge85]
GO:0003924 - GTPase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Dubnoff72]
GO:0005515 - protein binding Inferred from experiment [Helgstrand07]
GO:0043024 - ribosomal small subunit binding Inferred from experiment [Caserta06]
GO:0097216 - guanosine tetraphosphate binding Inferred from experiment [Milon06]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005525 - GTP binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0016020 - membrane Inferred from experiment [Lasserre06]
GO:0005622 - intracellular Inferred by computational analysis [GOA01a]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: information transfer protein related translation

Essentiality data for infB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Last-Curated ? 19-Jan-2012 by Keseler I , SRI International

Sequence Features

Protein sequence of protein chain initiation factor IF2 with features indicated

Feature Class Location Citations Comment
Intrinsic-Sequence-Variant 1 -> 157
Protein-Segment 1 -> 103
UniProt: 1; Sequence Annotation Type: region of interest;
Protein-Segment 104 -> 287
UniProt: 2; Sequence Annotation Type: region of interest;
Intrinsic-Sequence-Variant 158
UniProt: In isoform Beta..
Protein-Segment 167 -> 214
UniProt: Ala/Arg/Glu/Lys-rich; Sequence Annotation Type: compositionally biased region;
Protein-Segment 288 -> 391
UniProt: 3; Sequence Annotation Type: region of interest;
Conserved-Region 389 -> 558
UniProt: tr-type G.
Nucleotide-Phosphate-Binding-Region 398 -> 405
UniProt: GTP; Non-Experimental Qualifier: by similarity;
Extrinsic-Sequence-Variant 409
UniProt: In strain: IQ489..
Extrinsic-Sequence-Variant 423
UniProt: In strain: IQ490..
Protein-Segment 423 -> 427
UniProt: G2; Sequence Annotation Type: region of interest.
Extrinsic-Sequence-Variant 432
UniProt: In strain: ECOAU9326..
Protein-Segment 444 -> 447
UniProt: G3; Sequence Annotation Type: region of interest.
Nucleotide-Phosphate-Binding-Region 444 -> 448
UniProt: GTP; Non-Experimental Qualifier: by similarity;
Extrinsic-Sequence-Variant 490
UniProt: In strain: ECOAU9302, ECOAU9306, ECOAU9307 and ECOAU9309..
Nucleotide-Phosphate-Binding-Region 498 -> 501
UniProt: GTP; Non-Experimental Qualifier: by similarity;
Protein-Segment 534 -> 536
UniProt: G5; Sequence Annotation Type: region of interest.
Protein-Segment 541 -> 668
UniProt: 5; Sequence Annotation Type: region of interest;
Protein-Segment 669 -> 890
UniProt: 6; Sequence Annotation Type: region of interest;
Extrinsic-Sequence-Variant 684
UniProt: In strain: ECOAU9306..
N6-acetyllysine-Modification 808
[Zhang09a, UniProt15]
UniProt: N6-acetyllysine.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram


10/20/97 Gene b3168 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10505; confirmed by SwissProt match.


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Antoun03: Antoun A, Pavlov MY, Andersson K, Tenson T, Ehrenberg M (2003). "The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis." EMBO J 22(20);5593-601. PMID: 14532131

Antoun06: Antoun A, Pavlov MY, Lovmar M, Ehrenberg M (2006). "How initiation factors maximize the accuracy of tRNA selection in initiation of bacterial protein synthesis." Mol Cell 23(2);183-93. PMID: 16857585

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

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Benne73: Benne R, Naaktgeboren N, Gubbens J, Voorma HO (1973). "Recycling of initiation factors IF-1, IF-2 and IF-3." Eur J Biochem 32(2);372-80. PMID: 4569079

Berthelot77: Berthelot F, Bogdanovsky D, Schapira G, Gros F (1977). "Comparative nature of the reactions catalysed by reticulocyte initiation factor IF-M1 and Escherichia coli factor IF2 on Escherichia coli ribosomes." FEBS Lett 74(1);91-4. PMID: 320048

Boelens02: Boelens R, Gualerzi CO (2002). "Structure and function of bacterial initiation factors." Curr Protein Pept Sci 3(1);107-19. PMID: 12370015

Boileau83: Boileau G, Butler P, Hershey JW, Traut RR (1983). "Direct cross-links between initiation factors 1, 2, and 3 and ribosomal proteins promoted by 2-iminothiolane." Biochemistry 22(13);3162-70. PMID: 6349681

Brandi04: Brandi L, Marzi S, Fabbretti A, Fleischer C, Hill WE, Gualerzi CO, Stephen Lodmell J (2004). "The translation initiation functions of IF2: targets for thiostrepton inhibition." J Mol Biol 335(4);881-94. PMID: 14698286

Burakovskii07: Burakovskii DE, Smirnova AS, Lesniak DV, Kiparisov SV, Leonov AA, Sergiev PV, Bogdanov AA, Dontsova OA (2007). "[Interaction of 23S ribosomal RNA helices 89 and 91 of Escherichia coli contributes to the activity of IF2 but is insignificant for elongation factors functioning]." Mol Biol (Mosk) 41(6);1031-41. PMID: 18318122

Caldas00: Caldas T, Laalami S, Richarme G (2000). "Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2." J Biol Chem 275(2);855-60. PMID: 10625618

Caldon01: Caldon CE, Yoong P, March PE (2001). "Evolution of a molecular switch: universal bacterial GTPases regulate ribosome function." Mol Microbiol 41(2);289-97. PMID: 11489118

Cameron02: Cameron DM, Thompson J, March PE, Dahlberg AE (2002). "Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome." J Mol Biol 319(1);27-35. PMID: 12051934

Canonaco86: Canonaco MA, Calogero RA, Gualerzi CO (1986). "Mechanism of translational initiation in prokaryotes. Evidence for a direct effect of IF2 on the activity of the 30 S ribosomal subunit." FEBS Lett 207(2);198-204. PMID: 3533628

Caserta06: Caserta E, Tomsic J, Spurio R, La Teana A, Pon CL, Gualerzi CO (2006). "Translation initiation factor IF2 interacts with the 30 S ribosomal subunit via two separate binding sites." J Mol Biol 362(4);787-99. PMID: 16935296

Cenatiempo87: Cenatiempo Y, Deville F, Dondon J, Grunberg-Manago M, Sacerdot C, Hershey JW, Hansen HF, Petersen HU, Clark BF, Kjeldgaard M (1987). "The protein synthesis initiation factor 2 G-domain. Study of a functionally active C-terminal 65-kilodalton fragment of IF2 from Escherichia coli." Biochemistry 26(16);5070-6. PMID: 2444251

Cole87a: Cole JR, Olsson CL, Hershey JW, Grunberg-Manago M, Nomura M (1987). "Feedback regulation of rRNA synthesis in Escherichia coli. Requirement for initiation factor IF2." J Mol Biol 198(3);383-92. PMID: 2448483

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Dubnoff69: Dubnoff JS, Maitra U (1969). "Protein factors involved in polypeptide chain initiation in Escherichia coli." Cold Spring Harb Symp Quant Biol 34;301-6. PMID: 4314905

Dubnoff72: Dubnoff JS, Maitra U (1972). "Characterization of the ribosome-dependent guanosine triphosphatase activity of polypeptide chain initiation factor IF 2." J Biol Chem 247(9);2876-83. PMID: 4337107

Fakunding73: Fakunding JL, Traut RR, Hershey JW (1973). "Dependence of initiation factor IF-2 activity on proteins L7 and L12 from Escherichia coli 50 S ribosomes." J Biol Chem 248(24);8555-9. PMID: 4587128

Fakunding73a: Fakunding JL, Hershey JW (1973). "The interaction of radioactive initiation factor IF-2 with ribosomes during initiation of protein synthesis." J Biol Chem 248(12);4206-12. PMID: 4197131

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Grill00: Grill S, Gualerzi CO, Londei P, Blasi U (2000). "Selective stimulation of translation of leaderless mRNA by initiation factor 2: evolutionary implications for translation." EMBO J 19(15);4101-10. PMID: 10921890

Grill01: Grill S, Moll I, Hasenohrl D, Gualerzi CO, Blasi U (2001). "Modulation of ribosomal recruitment to 5'-terminal start codons by translation initiation factors IF2 and IF3." FEBS Lett 495(3);167-71. PMID: 11334885

Guillon96: Guillon JM, Heiss S, Soutourina J, Mechulam Y, Laalami S, Grunberg-Manago M, Blanquet S (1996). "Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli." J Biol Chem 271(37);22321-5. PMID: 8798391

Hamel75: Hamel E (1975). "Activities of guanosine triphosphate analogues in reactions catalyzed by elongation factor Tu and initiation factor 2 of Escherichia coli." Biochim Biophys Acta 414(3);326-40. PMID: 1106767

Hartz89: Hartz D, McPheeters DS, Gold L (1989). "Selection of the initiator tRNA by Escherichia coli initiation factors." Genes Dev 3(12A);1899-912. PMID: 2695390

Heimark76: Heimark RL, Hershey JW, Traut RR (1976). "Cross-linking of initiation factor IF2 to proteins L7/L12 in 70 S ribosomes of Escherichia coli." J Biol Chem 251(24);7779-84. PMID: 826536

Helgstrand07: Helgstrand M, Mandava CS, Mulder FA, Liljas A, Sanyal S, Akke M (2007). "The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 C-terminal domain." J Mol Biol 365(2);468-79. PMID: 17070545

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Iwasaki68: Iwasaki K, Sabol S, Wahba AJ, Ochoa S (1968). "Translation of the genetic message. VII. Role of initiation factors in formation of the chain initiation complex with Escherichia coli ribosomes." Arch Biochem Biophys 125(2);542-7. PMID: 4872321

Julian11: Julian P, Milon P, Agirrezabala X, Lasso G, Gil D, Rodnina MV, Valle M (2011). "The Cryo-EM structure of a complete 30S translation initiation complex from Escherichia coli." PLoS Biol 9(7);e1001095. PMID: 21750663

Karimi98: Karimi R, Pavlov MY, Heurgue-Hamard V, Buckingham RH, Ehrenberg M (1998). "Initiation factors IF1 and IF2 synergistically remove peptidyl-tRNAs with short polypeptides from the P-site of translating Escherichia coli ribosomes." J Mol Biol 281(2);241-52. PMID: 9698545

Kolakofsky68: Kolakofsky D, Dewey KF, Hershey JW, Thach RE (1968). "Guanosine 5'-triphosphatase activity of initiation factor f2." Proc Natl Acad Sci U S A 61(3);1066-70. PMID: 5246542

Krauss75: Krauss SW, Leder P (1975). "Regulation of initiation and elongation factor levels in Escherichia coli as assessed by a quantitative immunoassay." J Biol Chem 250(10);3752-8. PMID: 805131

La01: La Teana A, Gualerzi CO, Dahlberg AE (2001). "Initiation factor IF 2 binds to the alpha-sarcin loop and helix 89 of Escherichia coli 23S ribosomal RNA." RNA 7(8);1173-9. PMID: 11497435

La93: La Teana A, Pon CL, Gualerzi CO (1993). "Translation of mRNAs with degenerate initiation triplet AUU displays high initiation factor 2 dependence and is subject to initiation factor 3 repression." Proc Natl Acad Sci U S A 90(9);4161-5. PMID: 8483930

Laalami91: Laalami S, Putzer H, Plumbridge JA, Grunberg-Manago M (1991). "A severely truncated form of translational initiation factor 2 supports growth of Escherichia coli." J Mol Biol 220(2);335-49. PMID: 1830345

Laalami91a: Laalami S, Sacerdot C, Vachon G, Mortensen K, Sperling-Petersen HU, Cenatiempo Y, Grunberg-Manago M (1991). "Structural and functional domains of E coli initiation factor IF2." Biochimie 73(12);1557-66. PMID: 1805969

Laalami94: Laalami S, Timofeev AV, Putzer H, Leautey J, Grunberg-Manago M (1994). "In vivo study of engineered G-domain mutants of Escherichia coli translation initiation factor IF2." Mol Microbiol 11(2);293-302. PMID: 8170391

Larigauderie00: Larigauderie G, Laalami S, Nyengaard NR, Grunberg-Manago M, Cenatiempo Y, Mortensen KK, Sperling-Petersen HU (2000). "Mutation of Thr445 and Ile500 of initiation factor 2 G-domain affects Escherichia coli growth rate at low temperature." Biochimie 82(12);1091-8. PMID: 11120350

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Laursen03: Laursen BS, Siwanowicz I, Larigauderie G, Hedegaard J, Ito K, Nakamura Y, Kenney JM, Mortensen KK, Sperling-Petersen HU (2003). "Characterization of mutations in the GTP-binding domain of IF2 resulting in cold-sensitive growth of Escherichia coli." J Mol Biol 326(2);543-51. PMID: 12559921

Laursen03a: Laursen BS, Mortensen KK, Sperling-Petersen HU, Hoffman DW (2003). "A conserved structural motif at the N terminus of bacterial translation initiation factor IF2." J Biol Chem 278(18);16320-8. PMID: 12600987

Laursen04: Laursen BS, Kjaergaard AC, Mortensen KK, Hoffman DW, Sperling-Petersen HU (2004). "The N-terminal domain (IF2N) of bacterial translation initiation factor IF2 is connected to the conserved C-terminal domains by a flexible linker." Protein Sci 13(1);230-9. PMID: 14691238

Laursen05: Laursen BS, Sorensen HP, Mortensen KK, Sperling-Petersen HU (2005). "Initiation of protein synthesis in bacteria." Microbiol Mol Biol Rev 69(1);101-23. PMID: 15755955

Lelong70: Lelong JC, Grunberg-Manago M, Dondon J, Gros D, Gros F (1970). "Interaction between guanosine derivatives and factors involved in the initiation of protein synthesis." Nature 226(5245);505-10. PMID: 4909915

Lockwood71: Lockwood AH, Chakraborty PR, Maitra U (1971). "A complex between initiation factor IF2, guanosine triphosphate, and fMet-tRNA: an intermediate in initiation complex formation." Proc Natl Acad Sci U S A 68(12);3122-6. PMID: 4943554

Lockwood72: Lockwood AH, Sarkar P, Maitra U (1972). "Release of polypeptide chain initiation factor IF-2 during initiation complex formation." Proc Natl Acad Sci U S A 69(12);3602-5. PMID: 4566451

Luchin99: Luchin S, Putzer H, Hershey JW, Cenatiempo Y, Grunberg-Manago M, Laalami S (1999). "In vitro study of two dominant inhibitory GTPase mutants of Escherichia coli translation initiation factor IF2. Direct evidence that GTP hydrolysis is necessary for factor recycling." J Biol Chem 274(10);6074-9. PMID: 10037688

Majumdar76: Majumdar A, Bose KK, Gupta NK (1976). "Specific binding of Excherichia coli chain Initiation factor 2 to fMet-tRnafMet." J Biol Chem 251(1);137-40. PMID: 1104625

Mandava12: Mandava CS, Peisker K, Ederth J, Kumar R, Ge X, Szaflarski W, Sanyal S (2012). "Bacterial ribosome requires multiple L12 dimers for efficient initiation and elongation of protein synthesis involving IF2 and EF-G." Nucleic Acids Res 40(5);2054-64. PMID: 22102582

Mangroo95: Mangroo D, RajBhandary UL (1995). "Mutants of Escherichia coli initiator tRNA defective in initiation. Effects of overproduction of methionyl-tRNA transformylase and the initiation factors IF2 and IF3." J Biol Chem 270(20);12203-9. PMID: 7538134

Mayer03: Mayer C, Kohrer C, Kenny E, Prusko C, RajBhandary UL (2003). "Anticodon sequence mutants of Escherichia coli initiator tRNA: effects of overproduction of aminoacyl-tRNA synthetases, methionyl-tRNA formyltransferase, and initiation factor 2 on activity in initiation." Biochemistry 42(17);4787-99. PMID: 12718519

Mazumder72: Mazumder R (1972). "Initiation factor 2-dependent ribosomal binding of N-formylmethionyl-transfer RNA without added guanosine triphosphate." Proc Natl Acad Sci U S A 69(10);2770-3. PMID: 4562740

Mechulam11: Mechulam Y, Blanquet S, Schmitt E (2011). "Translation Initiation." EcoSal online edition, Module 4.2.2.

Miller73a: Miller MJ, Wahba AJ (1973). "Chain initiation factor 2. Purification and properties of two species from Escherichia coli MRE 600." J Biol Chem 248(3);1084-90. PMID: 4567787

Milon06: Milon P, Tischenko E, Tomsic J, Caserta E, Folkers G, La Teana A, Rodnina MV, Pon CL, Boelens R, Gualerzi CO (2006). "The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor." Proc Natl Acad Sci U S A 103(38);13962-7. PMID: 16968770

Milon07: Milon P, Konevega AL, Peske F, Fabbretti A, Gualerzi CO, Rodnina MV (2007). "Transient kinetics, fluorescence, and FRET in studies of initiation of translation in bacteria." Methods Enzymol 430;1-30. PMID: 17913632

Moll02: Moll I, Grill S, Gualerzi CO, Blasi U (2002). "Leaderless mRNAs in bacteria: surprises in ribosomal recruitment and translational control." Mol Microbiol 43(1);239-46. PMID: 11849551

MorelDeville90: Morel-Deville F, Vachon G, Sacerdot C, Cozzone AJ, Grunberg-Manago M, Cenatiempo Y (1990). "Characterization of the translational start site for IF2 beta, a short form of Escherichia coli initiation factor IF2." Eur J Biochem 188(3);605-14. PMID: 2110058

Moreno98: Moreno JM, Kildsgaard J, Siwanowicz I, Mortensen KK, Sperling-Petersen HU (1998). "Binding of Escherichia coli initiation factor IF2 to 30S ribosomal subunits: a functional role for the N-terminus of the factor." Biochem Biophys Res Commun 252(2);465-71. PMID: 9826553

Moreno99: Moreno JM, Drskjotersen L, Kristensen JE, Mortensen KK, Sperling-Petersen HU (1999). "Characterization of the domains of E. coli initiation factor IF2 responsible for recognition of the ribosome." FEBS Lett 455(1-2);130-4. PMID: 10428486

Mortensen95: Mortensen KK, Hajnsdorf E, Regnier P, Sperling-Petersen HU (1995). "Improved recombinant tandem expression of translation initiation factor IF2 in RNASE E deficient E. coli cells." Biochem Biophys Res Commun 214(3);1254-9. PMID: 7575538

Naaktgeboren75: Naaktgeboren N, Vermaas A, Voorma HO (1975). "The joining of the 30-S initiation complex with the 50-S subunit, the main target for thiostrepton." Eur J Biochem 57(2);493-51. PMID: 1100407

Nakamura85: Nakamura Y, Mizusawa S (1985). "In vivo evidence that the nusA and infB genes of E. coli are part of the same multi-gene operon which encodes at least four proteins." EMBO J 1985;4(2);527-32. PMID: 2990900

Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.

North07: North SH, Kirtland SE, Nakai H (2007). "Translation factor IF2 at the interface of transposition and replication by the PriA-PriC pathway." Mol Microbiol 66(6);1566-78. PMID: 18028309

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Petersen79: Petersen HU, Roll T, Grunberg-Manago M, Clark BF (1979). "Specific interaction of initiation factor IF2 of E. coli with formylmethionyl-tRNA f Met." Biochem Biophys Res Commun 91(3);1068-74. PMID: 393258

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Plumbridge85: Plumbridge JA, Deville F, Sacerdot C, Petersen HU, Cenatiempo Y, Cozzone A, Grunberg-Manago M, Hershey JW (1985). "Two translational initiation sites in the infB gene are used to express initiation factor IF2 alpha and IF2 beta in Escherichia coli." EMBO J 4(1);223-9. PMID: 3894004

Pon85: Pon CL, Paci M, Pawlik RT, Gualerzi CO (1985). "Structure-function relationship in Escherichia coli initiation factors. Biochemical and biophysical characterization of the interaction between IF-2 and guanosine nucleotides." J Biol Chem 260(15);8918-24. PMID: 3894350

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Regnier89: Regnier P, Grunberg-Manago M (1989). "Cleavage by RNase III in the transcripts of the met Y-nus-A-infB operon of Escherichia coli releases the tRNA and initiates the decay of the downstream mRNA." J Mol Biol 210(2);293-302. PMID: 2481042

Regnier90: Regnier P, Grunberg-Manago M (1990). "RNase III cleavages in non-coding leaders of Escherichia coli transcripts control mRNA stability and genetic expression." Biochimie 72(11);825-34. PMID: 2085545

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Sacerdot84: Sacerdot C, Dessen P, Hershey JW, Plumbridge JA, Grunberg-Manago M (1984). "Sequence of the initiation factor IF2 gene: unusual protein features and homologies with elongation factors." Proc Natl Acad Sci U S A 81(24);7787-91. PMID: 6096856

Sacerdot92: Sacerdot C, Vachon G, Laalami S, Morel-Deville F, Cenatiempo Y, Grunberg-Manago M (1992). "Both forms of translational initiation factor IF2 (alpha and beta) are required for maximal growth of Escherichia coli. Evidence for two translational initiation codons for IF2 beta." J Mol Biol 225(1);67-80. PMID: 1374802

Sands88: Sands JF, Regnier P, Cummings HS, Grunberg-Manago M, Hershey JW (1988). "The existence of two genes between infB and rpsO in the Escherichia coli genome: DNA sequencing and S1 nuclease mapping." Nucleic Acids Res 1988;16(22);10803-16. PMID: 2849753

Schmitt80: Schmitt M, Manderschied U, Kyriatsoulis A, Brinckmann U, Gassen HG (1980). "Tetranucleotides as effectors for the binding of initiator tRNA to Escherichia coli ribosomes." Eur J Biochem 109(1);291-9. PMID: 6997046

Schmitt96: Schmitt E, Guillon JM, Meinnel T, Mechulam Y, Dardel F, Blanquet S (1996). "Molecular recognition governing the initiation of translation in Escherichia coli. A review." Biochimie 78(7);543-54. PMID: 8955898

Shiba86: Shiba K, Ito K, Nakamura Y, Dondon J, Grunberg-Manago M (1986). "Altered translation initiation factor 2 in the cold-sensitive ssyG mutant affects protein export in Escherichia coli." EMBO J 5(11);3001-6. PMID: 3539591

Steffensen97: Steffensen SA, Poulsen AB, Mortensen KK, Sperling-Petersen HU (1997). "E. coli translation initiation factor IF2--an extremely conserved protein. Comparative sequence analysis of the infB gene in clinical isolates of E. coli." FEBS Lett 419(2-3);281-4. PMID: 9428651

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UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

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UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

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UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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vanderHofstad78: van der Hofstad GA, Buitenhek A, Bosch L, Voorma HO (1978). "Initiation factor IF-3 and the binary complex between initiation factor IF-2 and formylmethionyl-tRNA are mutually exclusive on the 30-S ribosomal subunit." Eur J Biochem 89(1);213-20. PMID: 359327

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Other References Related to Gene Regulation

Caldara06: Caldara M, Charlier D, Cunin R (2006). "The arginine regulon of Escherichia coli: whole-system transcriptome analysis discovers new genes and provides an integrated view of arginine regulation." Microbiology 152(Pt 11);3343-54. PMID: 17074904

Charlier92: Charlier D, Roovers M, Van Vliet F, Boyen A, Cunin R, Nakamura Y, Glansdorff N, Pierard A (1992). "Arginine regulon of Escherichia coli K-12. A study of repressor-operator interactions and of in vitro binding affinities versus in vivo repression." J Mol Biol 1992;226(2);367-86. PMID: 1640456

Granston90: Granston AE, Thompson DL, Friedman DI (1990). "Identification of a second promoter for the metY-nusA-infB operon of Escherichia coli." J Bacteriol 172(5);2336-42. PMID: 1692017

Ishii84: Ishii S, Kuroki K, Imamoto F (1984). "tRNAMetf2 gene in the leader region of the nusA operon in Escherichia coli." Proc Natl Acad Sci U S A 1984;81(2);409-13. PMID: 6364142

Krin03: Krin E, Laurent-Winter C, Bertin PN, Danchin A, Kolb A (2003). "Transcription regulation coupling of the divergent argG and metY promoters in Escherichia coli K-12." J Bacteriol 185(10);3139-46. PMID: 12730174

Maciag11a: Maciag A, Peano C, Pietrelli A, Egli T, De Bellis G, Landini P (2011). "In vitro transcription profiling of the {sigma}S subunit of bacterial RNA polymerase: re-definition of the {sigma}S regulon and identification of {sigma}S-specific promoter sequence elements." Nucleic Acids Res 39(13);5338-55. PMID: 21398637

Makarova01: Makarova KS, Mironov AA, Gelfand MS (2001). "Conservation of the binding site for the arginine repressor in all bacterial lineages." Genome Biol 2(4);RESEARCH0013. PMID: 11305941

Regnier87: Regnier P, Grunberg-Manago M, Portier C (1987). "Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1." J Biol Chem 1987;262(1);63-8. PMID: 2432069

Shimada13: Shimada T, Yoshida H, Ishihama A (2013). "Involvement of cyclic AMP receptor protein in regulation of the rmf gene encoding the ribosome modulation factor in Escherichia coli." J Bacteriol 195(10);2212-9. PMID: 23475967

Zaslaver06: Zaslaver A, Bren A, Ronen M, Itzkovitz S, Kikoin I, Shavit S, Liebermeister W, Surette MG, Alon U (2006). "A comprehensive library of fluorescent transcriptional reporters for Escherichia coli." Nat Methods 3(8);623-8. PMID: 16862137

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