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Escherichia coli K-12 substr. MG1655 Polypeptide: 30S ribosomal subunit protein S6



Gene: rpsF Accession Numbers: EG10905 (EcoCyc), b4200, ECK4196

Synonyms: sdgH

Regulation Summary Diagram: ?

Component of:
30S ribosomal subunit (summary available)
ribosome (summary available)

Summary:
The S6 protein is a component of the 30S subunit of the ribosome. S6 interacts with the central domain of 16S rRNA [Gregory84, Stern88].

The S6 protein contains glutamate residues at the C-terminus, only two of which are encoded by the rpsF gene [Reeh79, Schnier86]; up to four additional glutamate residues are added post-translationally by the RimK enzyme [Kang89]. This form of S6 accumulates when the soxR regulon is activated [Greenberg90]. In bacteriophage T7-infected cells, S6 is phosphorylated [Robertson94].

Expression analysis of rpsFp indicates that it may be autoregulated by one or more of its operon components [Nakayashiki13]. Coexpressed S6:S18 were found to bind to the rpsF 5'-UTR in a region with structural similarity to their binding site in 16S rRNA. S6 together with S18 may thus be responsible for autoregulation of the rpsF-priB-rpsR-rplI operon [Matelska13].

A class of mutations in rpsF supresses the temperature-sensitive growth defect of certain dnaG alleles [Britton97]. The rpsF292 allele, which introduces a stop codon in place of Glu98, is an effective suppressor of ΔrecG. The effect is due to both elimination of RpsF and lower expression of PriB [Mahdi12]. Both rimK and rpsF deletion mutants reduce the basal level of SOS response and increase resistance to hydroxyurea [Nakayashiki13].

SdgH: "supressor of dnaG" [Britton97]

Review: [Nesterchuk11]

Citations: [Mulder10, Tang14]

Gene Citations: [Allen91]

Locations: cytosol, ribosome

Map Position: [4,423,141 -> 4,423,536] (95.33 centisomes)
Length: 396 bp / 131 aa

Molecular Weight of Polypeptide: 15.187 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0013740 , CGSC:225 , DIP:DIP-10782N , EchoBASE:EB0898 , EcoGene:EG10905 , EcoliWiki:b4200 , Mint:MINT-1279331 , ModBase:P02358 , OU-Microarray:b4200 , PortEco:rpsF , PR:PRO_000023859 , Pride:P02358 , Protein Model Portal:P02358 , RefSeq:NP_418621 , RegulonDB:EG10905 , SMR:P02358 , String:511145.b4200 , UniProt:P02358

Relationship Links: InterPro:IN-FAMILY:IPR000529 , InterPro:IN-FAMILY:IPR014717 , InterPro:IN-FAMILY:IPR020814 , InterPro:IN-FAMILY:IPR020815 , PDB:Structure:1EG0 , PDB:Structure:1M5G , PDB:Structure:1P6G , PDB:Structure:1P87 , PDB:Structure:1VS5 , PDB:Structure:1VS7 , PDB:Structure:2AVY , PDB:Structure:2AW7 , PDB:Structure:2GY9 , PDB:Structure:2GYB , PDB:Structure:2I2P , PDB:Structure:2I2U , PDB:Structure:2QAL , PDB:Structure:2QAN , PDB:Structure:2QB9 , PDB:Structure:2QBB , PDB:Structure:2QBD , PDB:Structure:2QBF , PDB:Structure:2QBH , PDB:Structure:2QBJ , PDB:Structure:2QOU , PDB:Structure:2QOW , PDB:Structure:2QOY , PDB:Structure:2QP0 , PDB:Structure:2VHO , PDB:Structure:2VHP , PDB:Structure:2WWL , PDB:Structure:2YKR , PDB:Structure:2Z4K , PDB:Structure:2Z4M , PDB:Structure:3DF1 , PDB:Structure:3DF3 , PDB:Structure:3E1A , PDB:Structure:3E1C , PDB:Structure:3FIH , PDB:Structure:3I1M , PDB:Structure:3I1O , PDB:Structure:3I1Q , PDB:Structure:3I1S , PDB:Structure:3I1Z , PDB:Structure:3I21 , PDB:Structure:3IY8 , PDB:Structure:3IZV , PDB:Structure:3IZW , PDB:Structure:3J00 , PDB:Structure:3J0U , PDB:Structure:3J0V , PDB:Structure:3J0X , PDB:Structure:3J0Z , PDB:Structure:3J10 , PDB:Structure:3J13 , PDB:Structure:3J18 , PDB:Structure:3J36 , PDB:Structure:3KC4 , PDB:Structure:3OAQ , PDB:Structure:3OAR , PDB:Structure:3OFA , PDB:Structure:3OFB , PDB:Structure:3OFO , PDB:Structure:3OFP , PDB:Structure:3OFX , PDB:Structure:3OFY , PDB:Structure:3OR9 , PDB:Structure:3ORA , PDB:Structure:3SFS , PDB:Structure:3UOQ , PDB:Structure:4A2I , PDB:Structure:4ADV , PDB:Structure:4GAQ , PDB:Structure:4GAS , PDB:Structure:4GD1 , PDB:Structure:4GD2 , PDB:Structure:4KIY , PDB:Structure:4KJ0 , PDB:Structure:4KJ2 , PDB:Structure:4KJ4 , PDB:Structure:4KJ6 , PDB:Structure:4KJ8 , PDB:Structure:4KJA , PDB:Structure:4KJC , Pfam:IN-FAMILY:PF01250 , Prosite:IN-FAMILY:PS01048

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006412 - translation Inferred by computational analysis [GOA06, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Zheng11, Hauser14, Rajagopala14]
GO:0048027 - mRNA 5'-UTR binding Inferred from experiment [Matelska13]
GO:0070181 - small ribosomal subunit rRNA binding Inferred from experiment [Gregory84]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0022627 - cytosolic small ribosomal subunit Inferred from experiment [Hindennach71a, WittmannLiebold73]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation

Essentiality data for rpsF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Indeterminate 37 Aerobic 7   Yes [Baba06, Comment 1]
Low [Bubunenko07]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]

Credits:
Last-Curated ? 22-Nov-2013 by Keseler I , SRI International


Subunit of: 30S ribosomal subunit

Synonyms: ribosome, small subunit

Subunit composition of 30S ribosomal subunit = [RrsA][RpsA][RpsB][RpsC][RpsD][RpsE][RpsF][RpsG][RpsH][RpsI][RpsJ][RpsK][RpsL][RpsM][RpsN][RpsO][RpsP][RpsQ][RpsR][RpsS][RpsT][RpsU][Sra]
         16S ribosomal RNA (rrsA) = RrsA (extended summary available)
         30S ribosomal subunit protein S1 = RpsA (extended summary available)
         30S ribosomal subunit protein S2 = RpsB (summary available)
         30S ribosomal subunit protein S3 = RpsC (summary available)
         30S ribosomal subunit protein S4 = RpsD (extended summary available)
         30S ribosomal subunit protein S5 = RpsE (extended summary available)
         30S ribosomal subunit protein S6 = RpsF (extended summary available)
         30S ribosomal subunit protein S7 = RpsG (extended summary available)
         30S ribosomal subunit protein S8 = RpsH (extended summary available)
         30S ribosomal subunit protein S9 = RpsI (extended summary available)
         30S ribosomal subunit protein S10 = RpsJ (extended summary available)
         30S ribosomal subunit protein S11 = RpsK (summary available)
         30S ribosomal subunit protein S12 = RpsL (extended summary available)
         30S ribosomal subunit protein S13 = RpsM (extended summary available)
         30S ribosomal subunit protein S14 = RpsN (summary available)
         30S ribosomal subunit protein S15 = RpsO (extended summary available)
         30S ribosomal subunit protein S16 = RpsP (summary available)
         30S ribosomal subunit protein S17 = RpsQ (summary available)
         30S ribosomal subunit protein S18 = RpsR (extended summary available)
         30S ribosomal subunit protein S19 = RpsS (summary available)
         30S ribosomal subunit protein S20 = RpsT (extended summary available)
         30S ribosomal subunit protein S21 = RpsU (summary available)
         30S ribosomal subunit protein S22 = Sra (summary available)

Component of: ribosome (summary available)

Summary:
Assembly of the 30S ribosomal subunit has been studied in real time. Initial assembly is linked to the formation of structured 16S rRNA regions, while later steps involve induced fit between ribosomal proteins and the rRNA [Adilakshmi08]. Discovery single-particle profiling was used to visualize assembly of the 30S ribosomal subunit by indentifying and following changes among 14 subunit assembly intermediates over time [Mulder10]. The kinetically favored assembly pathway of the 30S preinitiation complex has been determined [Milon12].

The function of the ribosomal P site has been reviewed [Noller05].

Relationship Links: PDB:Structure:1P6G , PDB:Structure:1P87 , PDB:Structure:2AVY

Enzymes activated by 30S ribosomal subunit, sorted by the type of activation, are:

Activator (Mechanism unknown) of: GTPase [Daigle04, Himeno04]

Credits:
Created 28-Mar-2006 by Keseler I , SRI International


Subunit of: ribosome

Subunit composition of ribosome = [(RrsA)(RpsA)(RpsB)(RpsC)(RpsD)(RpsE)(RpsF)(RpsG)(RpsH)(RpsI)(RpsJ)(RpsK)(RpsL)(RpsM)(RpsN)(RpsO)(RpsP)(RpsQ)(RpsR)(RpsS)(RpsT)(RpsU)(Sra)][(RrlA)(RrfA)(RplA)(RplB)(RplC)(RplD)(RplE)(RplF)([RplJ][(RplL)2]2)(RplI)(RplK)(RplM)(RplN)(RplO)(RplP)(RplQ)(RplR)(RplS)(RplT)(RplU)(RplV)(RplW)(RplX)(RplY)(RpmA)(RpmB)(RpmC)(RpmD)(RpmE)(RpmF)(RpmG)(RpmH)(RpmI)(RpmJ)]
         30S ribosomal subunit = (RrsA)(RpsA)(RpsB)(RpsC)(RpsD)(RpsE)(RpsF)(RpsG)(RpsH)(RpsI)(RpsJ)(RpsK)(RpsL)(RpsM)(RpsN)(RpsO)(RpsP)(RpsQ)(RpsR)(RpsS)(RpsT)(RpsU)(Sra) (summary available)
                 16S ribosomal RNA (rrsA) = RrsA (extended summary available)
                 30S ribosomal subunit protein S1 = RpsA (extended summary available)
                 30S ribosomal subunit protein S2 = RpsB (summary available)
                 30S ribosomal subunit protein S3 = RpsC (summary available)
                 30S ribosomal subunit protein S4 = RpsD (extended summary available)
                 30S ribosomal subunit protein S5 = RpsE (extended summary available)
                 30S ribosomal subunit protein S6 = RpsF (extended summary available)
                 30S ribosomal subunit protein S7 = RpsG (extended summary available)
                 30S ribosomal subunit protein S8 = RpsH (extended summary available)
                 30S ribosomal subunit protein S9 = RpsI (extended summary available)
                 30S ribosomal subunit protein S10 = RpsJ (extended summary available)
                 30S ribosomal subunit protein S11 = RpsK (summary available)
                 30S ribosomal subunit protein S12 = RpsL (extended summary available)
                 30S ribosomal subunit protein S13 = RpsM (extended summary available)
                 30S ribosomal subunit protein S14 = RpsN (summary available)
                 30S ribosomal subunit protein S15 = RpsO (extended summary available)
                 30S ribosomal subunit protein S16 = RpsP (summary available)
                 30S ribosomal subunit protein S17 = RpsQ (summary available)
                 30S ribosomal subunit protein S18 = RpsR (extended summary available)
                 30S ribosomal subunit protein S19 = RpsS (summary available)
                 30S ribosomal subunit protein S20 = RpsT (extended summary available)
                 30S ribosomal subunit protein S21 = RpsU (summary available)
                 30S ribosomal subunit protein S22 = Sra (summary available)
         50S ribosomal subunit = (RrlA)(RrfA)(RplA)(RplB)(RplC)(RplD)(RplE)(RplF)([RplJ][(RplL)2]2)(RplI)(RplK)(RplM)(RplN)(RplO)(RplP)(RplQ)(RplR)(RplS)(RplT)(RplU)(RplV)(RplW)(RplX)(RplY)(RpmA)(RpmB)(RpmC)(RpmD)(RpmE)(RpmF)(RpmG)(RpmH)(RpmI)(RpmJ)
                 23S ribosomal RNA (rrlA) = RrlA (extended summary available)
                 5S ribosomal RNA (rrfA) = RrfA (extended summary available)
                 50S ribosomal subunit protein L1 = RplA (extended summary available)
                 50S ribosomal subunit protein L2 = RplB (summary available)
                 50S ribosomal subunit protein L3 = RplC (summary available)
                 50S ribosomal subunit protein L4 = RplD (extended summary available)
                 50S ribosomal subunit protein L5 = RplE (summary available)
                 50S ribosomal subunit protein L6 = RplF (summary available)
                 50S ribosomal protein complex L8 = (RplJ)([RplL]2)2 (summary available)
                         50S ribosomal subunit protein L10 = RplJ (extended summary available)
                         50S ribosomal subunit protein L7/L12 dimer = (RplL)2
                                 50S ribosomal subunit protein L12 = RplL
                 50S ribosomal subunit protein L9 = RplI (summary available)
                 50S ribosomal subunit protein L11 = RplK (extended summary available)
                 50S ribosomal subunit protein L13 = RplM (extended summary available)
                 50S ribosomal subunit protein L14 = RplN (extended summary available)
                 50S ribosomal subunit protein L15 = RplO (summary available)
                 50S ribosomal subunit protein L16 = RplP (extended summary available)
                 50S ribosomal subunit protein L17 = RplQ (summary available)
                 50S ribosomal subunit protein L18 = RplR (extended summary available)
                 50S ribosomal subunit protein L19 = RplS (extended summary available)
                 50S ribosomal subunit protein L20 = RplT (extended summary available)
                 50S ribosomal subunit protein L21 = RplU (summary available)
                 50S ribosomal subunit protein L22 = RplV (extended summary available)
                 50S ribosomal subunit protein L23 = RplW (extended summary available)
                 50S ribosomal subunit protein L24 = RplX (summary available)
                 50S ribosomal subunit protein L25 = RplY (summary available)
                 50S ribosomal subunit protein L27 = RpmA (extended summary available)
                 50S ribosomal subunit protein L28 = RpmB (summary available)
                 50S ribosomal subunit protein L29 = RpmC (summary available)
                 50S ribosomal subunit protein L30 = RpmD (summary available)
                 50S ribosomal subunit protein L31 = RpmE (summary available)
                 50S ribosomal subunit protein L32 = RpmF (summary available)
                 50S ribosomal subunit protein L33 = RpmG (summary available)
                 50S ribosomal subunit protein L34 = RpmH (summary available)
                 50S ribosomal subunit protein L35 = RpmI (summary available)
                 50S ribosomal subunit protein L36 = RpmJ (summary available)

Summary:
The ribosome is a complex machinery that translates the genetic code.

A crystal structure of the E. coli ribosome has been determined at 3.5 Å resolution [Schuwirth05]. Additional crystal structures of the ribosome with tRNA bound in two functionally distinct states reveal how a ratchet-like motion of the small and large subunits contributes to translocation, termination of translation, and ribosome recycling [Zhang09a, Dunkle11].

Approximately eight molecules of Zn2+ are bound to the ribosome; therefore, it appears that a large fraction of intracellular Zn2+ is ribosome-associated [Hensley11].

Selected reviews: [Ramakrishnan02, Yonath05, Ogle05, Kaczanowska07]

Citations: [Kuhlenkoetter11]

Relationship Links: PDB:Structure:3R8N , PDB:Structure:3R8O , PDB:Structure:3R8S , PDB:Structure:3R8T

Credits:
Created 15-Jun-2006 by Keseler I , SRI International


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 14
[Wasinger98, UniProt10a]
Alternate sequence: Q → T; UniProt: (in Ref. 6; AA sequence);
Sequence-Conflict 20
[Wasinger98, UniProt10a]
Alternate sequence: G → A; UniProt: (in Ref. 6; AA sequence);
Acetylation-Modification 56
[Yu08]
 
Acetylation-Modification 93
[Zhang09, UniProt11]
UniProt: N6-acetyllysine.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b4200 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10905; confirmed by SwissProt match.


References

Adilakshmi08: Adilakshmi T, Bellur DL, Woodson SA (2008). "Concurrent nucleation of 16S folding and induced fit in 30S ribosome assembly." Nature 455(7217);1268-72. PMID: 18784650

Allen91: Allen GC, Kornberg A (1991). "The priB gene encoding the primosomal replication n protein of Escherichia coli." J Biol Chem 1991;266(18);11610-3. PMID: 1646811

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

Britton97: Britton RA, Lupski JR (1997). "Isolation and characterization of suppressors of two Escherichia coli dnaG mutations, dnaG2903 and parB." Genetics 145(4);867-75. PMID: 9093842

Bubunenko07: Bubunenko M, Baker T, Court DL (2007). "Essentiality of ribosomal and transcription antitermination proteins analyzed by systematic gene replacement in Escherichia coli." J Bacteriol 189(7);2844-53. PMID: 17277072

Daigle04: Daigle DM, Brown ED (2004). "Studies of the interaction of Escherichia coli YjeQ with the ribosome in vitro." J Bacteriol 186(5);1381-7. PMID: 14973029

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

Dunkle11: Dunkle JA, Wang L, Feldman MB, Pulk A, Chen VB, Kapral GJ, Noeske J, Richardson JS, Blanchard SC, Cate JH (2011). "Structures of the bacterial ribosome in classical and hybrid states of tRNA binding." Science 332(6032);981-4. PMID: 21596992

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."

Greenberg90: Greenberg JT, Monach P, Chou JH, Josephy PD, Demple B (1990). "Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli." Proc Natl Acad Sci U S A 87(16);6181-5. PMID: 1696718

Gregory84: Gregory RJ, Zeller ML, Thurlow DL, Gourse RL, Stark MJ, Dahlberg AE, Zimmermann RA (1984). "Interaction of ribosomal proteins S6, S8, S15 and S18 with the central domain of 16 S ribosomal RNA from Escherichia coli." J Mol Biol 178(2);287-302. PMID: 6208366

Hauser14: Hauser R, Ceol A, Rajagopala SV, Mosca R, Siszler G, Wermke N, Sikorski P, Schwarz F, Schick M, Wuchty S, Aloy P, Uetz P (2014). "A Second-generation Protein-Protein Interaction Network of Helicobacter pylori." Mol Cell Proteomics 13(5);1318-29. PMID: 24627523

Hensley11: Hensley MP, Tierney DL, Crowder MW (2011). "Zn(II) binding to Escherichia coli 70S ribosomes." Biochemistry 50(46);9937-9. PMID: 22026583

Himeno04: Himeno H, Hanawa-Suetsugu K, Kimura T, Takagi K, Sugiyama W, Shirata S, Mikami T, Odagiri F, Osanai Y, Watanabe D, Goto S, Kalachnyuk L, Ushida C, Muto A (2004). "A novel GTPase activated by the small subunit of ribosome." Nucleic Acids Res 32(17);5303-9. PMID: 15466596

Hindennach71a: Hindennach I, Stoffler G, Wittmann HG (1971). "Ribosomal proteins. Isolation of the proteins from 30S ribosomal subunits of Escherichia coli." Eur J Biochem 23(1);7-11. PMID: 4942549

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

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kaczanowska07: Kaczanowska M, Ryden-Aulin M (2007). "Ribosome biogenesis and the translation process in Escherichia coli." Microbiol Mol Biol Rev 71(3);477-94. PMID: 17804668

Kang89: Kang WK, Icho T, Isono S, Kitakawa M, Isono K (1989). "Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12." Mol Gen Genet 217(2-3);281-8. PMID: 2570347

Kuhlenkoetter11: Kuhlenkoetter S, Wintermeyer W, Rodnina MV (2011). "Different substrate-dependent transition states in the active site of the ribosome." Nature 476(7360);351-4. PMID: 21804565

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Mahdi12: Mahdi AA, Briggs GS, Lloyd RG (2012). "Modulation of DNA damage tolerance in Escherichia coli recG and ruv strains by mutations affecting PriB, the ribosome and RNA polymerase." Mol Microbiol 86(3);675-91. PMID: 22957744

Matelska13: Matelska D, Purta E, Panek S, Boniecki MJ, Bujnicki JM, Dunin-Horkawicz S (2013). "S6:S18 ribosomal protein complex interacts with a structural motif present in its own mRNA." RNA 19(10);1341-8. PMID: 23980204

Milon12: Milon P, Maracci C, Filonava L, Gualerzi CO, Rodnina MV (2012). "Real-time assembly landscape of bacterial 30S translation initiation complex." Nat Struct Mol Biol 19(6);609-15. PMID: 22562136

Mulder10: Mulder AM, Yoshioka C, Beck AH, Bunner AE, Milligan RA, Potter CS, Carragher B, Williamson JR (2010). "Visualizing ribosome biogenesis: parallel assembly pathways for the 30S subunit." Science 330(6004);673-7. PMID: 21030658

Nakayashiki13: Nakayashiki T, Mori H (2013). "Genome-wide screening with hydroxyurea reveals a link between nonessential ribosomal proteins and reactive oxygen species production." J Bacteriol 195(6);1226-35. PMID: 23292777

Nesterchuk11: Nesterchuk MV, Sergiev PV, Dontsova OA (2011). "Posttranslational Modifications of Ribosomal Proteins in Escherichia coli." Acta Naturae 3(2);22-33. PMID: 22649682

Noller05: Noller HF, Hoang L, Fredrick K (2005). "The 30S ribosomal P site: a function of 16S rRNA." FEBS Lett 579(4);855-8. PMID: 15680962

Ogle05: Ogle JM, Ramakrishnan V (2005). "Structural insights into translational fidelity." Annu Rev Biochem 74;129-77. PMID: 15952884

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Ramakrishnan02: Ramakrishnan V (2002). "Ribosome structure and the mechanism of translation." Cell 108(4);557-72. PMID: 11909526

Reeh79: Reeh S, Pedersen S (1979). "Post-translational modification of Escherichia coli ribosomal protein S6." Mol Gen Genet 173(2);183-7. PMID: 386035

Robertson94: Robertson ES, Aggison LA, Nicholson AW (1994). "Phosphorylation of elongation factor G and ribosomal protein S6 in bacteriophage T7-infected Escherichia coli." Mol Microbiol 11(6);1045-57. PMID: 8022276

Schnier86: Schnier J, Kitakawa M, Isono K (1986). "The nucleotide sequence of an Escherichia coli chromosomal region containing the genes for ribosomal proteins S6, S18, L9 and an open reading frame." Mol Gen Genet 204(1);126-32. PMID: 3528756

Schuwirth05: Schuwirth BS, Borovinskaya MA, Hau CW, Zhang W, Vila-Sanjurjo A, Holton JM, Cate JH (2005). "Structures of the bacterial ribosome at 3.5 A resolution." Science 310(5749);827-34. PMID: 16272117

Stern88: Stern S, Powers T, Changchien LM, Noller HF (1988). "Interaction of ribosomal proteins S5, S6, S11, S12, S18 and S21 with 16 S rRNA." J Mol Biol 201(4);683-95. PMID: 2459389

Tang14: Tang X, Yin Y, Ge M, Chen D (2014). "[Antisense RNA mediated gene silencing of nonessential gene rpsF in Escherichia coli]." Wei Sheng Wu Xue Bao 54(4);449-54. PMID: 25007658

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Wasinger98: Wasinger VC, Humphery-Smith I (1998). "Small genes/gene-products in Escherichia coli K-12." FEMS Microbiol Lett 169(2);375-82. PMID: 9868784

WittmannLiebold73: Wittmann-Liebold B (1973). "Studies on the primary structure of 20 proteins from Escherichia coli ribosomes by means of an improved protein sequenator." FEBS Lett 36(3);247-9. PMID: 4587209

Yonath05: Yonath A (2005). "Antibiotics targeting ribosomes: resistance, selectivity, synergism and cellular regulation." Annu Rev Biochem 74;649-79. PMID: 16180279

Yu08: Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG (2008). "The diversity of lysine-acetylated proteins in Escherichia coli." J Microbiol Biotechnol 18(9);1529-36. PMID: 18852508

Zhang09: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

Zhang09a: Zhang W, Dunkle JA, Cate JH (2009). "Structures of the ribosome in intermediate states of ratcheting." Science 325(5943);1014-7. PMID: 19696352

Zheng11: Zheng C, Yang L, Hoopmann MR, Eng JK, Tang X, Weisbrod CR, Bruce JE (2011). "Cross-linking measurements of in vivo protein complex topologies." Mol Cell Proteomics 10(10);M110.006841. PMID: 21697552

Other References Related to Gene Regulation

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

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305

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


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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