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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: ?

Summary:
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, Plumbridge85a, 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 [Laursen04a]. 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 [Caldas00b]; interestingly, IF2 levels are increased under osmotic stress conditions [Weber06a].

infB is an essential gene [Laalami91]. The ssyG class of cold-sensitive mutations localizes to infB [Shiba86a]. 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, Schmitt96b, Rodnina00, Caldon01, Boelens02, Moll02a, 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, Cole87, 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)
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

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

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006184 - GTP catabolic process Inferred by computational analysis Inferred from experiment [Dubnoff72, GOA06, GOA01]
GO:0006413 - translational initiation Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA06, GOA01, Lockwood71]
GO:0006412 - translation Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0003743 - translation initiation factor activity Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA06, GOA01, Lockwood71, Iwasaki68, Revel68, Plumbridge85a]
GO:0003924 - GTPase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, 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 [UniProtGOA11]
GO:0005525 - GTP binding Inferred by computational analysis [UniProtGOA11, GOA01]
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 [GOA01]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, 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]

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


Sequence Features

Feature Class Location Citations Comment
Intrinsic-Sequence-Variant 1 -> 157
[UniProt10]
Alternate sequence: MTDVTIKTLAAERQTSVERLVQQFADAGIRKSADDSVSAQEKQTLIDHLNQKNSGPDKLTLQRKTRSTLNIPGTGGKSKSVQIEVRKKRTFVKRDPQEAERLAAEEQAQREAEEQARREAEESAKREAQQKAEREAAEQAKREAAEQAKREAAEKDK → missing; UniProt: (in isoform Beta);
Alternate sequence: MTDVTIKTLAAERQTSVERLVQQFADAGIRKSADDSVSAQEKQTLIDHLNQKNSGPDKLTLQRKTRSTLNIPGTGGKSKSVQIEVRKKRTFVKRDPQEAERLAAEEQAQREAEEQARREAEESAKREAQQKAEREAAEQAKREAAEQAKREAAEKDKVSNQQDD → missing; UniProt: (in isoform Beta');
Protein-Segment 1 -> 103
[UniProt10a]
UniProt: 1; Sequence Annotation Type: region of interest;
Protein-Segment 104 -> 287
[UniProt10a]
UniProt: 2; Sequence Annotation Type: region of interest;
Intrinsic-Sequence-Variant 158
[UniProt10]
Alternate sequence: V → M; UniProt: (in isoform Beta);
Protein-Segment 167 -> 214
[UniProt09]
UniProt: Ala/Arg/Glu/Lys-rich; Sequence Annotation Type: compositionally biased region;
Protein-Segment 288 -> 391
[UniProt10a]
UniProt: 3; Sequence Annotation Type: region of interest;
Protein-Segment 392 -> 540
[UniProt10a]
UniProt: G-domain; Sequence Annotation Type: region of interest;
Nucleotide-Phosphate-Binding-Region 398 -> 405
[UniProt10a]
UniProt: GTP; Non-Experimental Qualifier: by similarity;
Extrinsic-Sequence-Variant 409
[UniProt10]
Alternate sequence: D → E; UniProt: (in strain: IQ489);
Extrinsic-Sequence-Variant 423
[UniProt10]
Alternate sequence: G → GG; UniProt: (in strain: IQ490);
Extrinsic-Sequence-Variant 432
[UniProt10]
Alternate sequence: H → Q; UniProt: (in strain: ECOAU9326);
Nucleotide-Phosphate-Binding-Region 444 -> 448
[UniProt10a]
UniProt: GTP; Non-Experimental Qualifier: by similarity;
Extrinsic-Sequence-Variant 490
[UniProt10]
Alternate sequence: Q → G; UniProt: (in strain: ECOAU9302, ECOAU9306, ECOAU9307 and ECOAU9309);
Nucleotide-Phosphate-Binding-Region 498 -> 501
[UniProt10a]
UniProt: GTP; Non-Experimental Qualifier: by similarity;
Protein-Segment 541 -> 668
[UniProt10a]
UniProt: 5; Sequence Annotation Type: region of interest;
Protein-Segment 669 -> 890
[UniProt10a]
UniProt: 6; Sequence Annotation Type: region of interest;
Extrinsic-Sequence-Variant 684
[UniProt10]
Alternate sequence: G → A; UniProt: (in strain: ECOAU9306);
Acetylation-Modification 808
[Zhang09b, UniProt11]
UniProt: N6-acetyllysine.


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

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


References

Allen05: Allen GS, Zavialov A, Gursky R, Ehrenberg M, Frank J (2005). "The cryo-EM structure of a translation initiation complex from Escherichia coli." Cell 121(5);703-12. PMID: 15935757

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

Beaudry79: Beaudry P, Sander G, Grunberg-Manago M, Douzou P (1979). "Cation-induced regulatory mechanism of GTPase activity dependent on polypeptide initiation factor 2." Biochemistry 18(1);202-7. PMID: 217406

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

Caldas00b: 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

Cole87: 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

GOA01: 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

Laursen04a: 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

Moll02a: 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

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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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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

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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

Maciag11: 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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