Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
Updated BioCyc iOS App now
available in iTunes store
twitter

Escherichia coli K-12 substr. MG1655 Polypeptide: 50S ribosomal subunit protein L3



Gene: rplC Accession Numbers: EG10866 (EcoCyc), b3320, ECK3307

Regulation Summary Diagram

Regulation summary diagram for rplC

Component of:
50S ribosomal subunit
ribosome (summary available)

Summary:
The L3 protein is a component of the 50S subunit of the ribosome. L3 and L24 are the two proteins that initiate assembly of the 50S subunit [Nowotny82].

The L3 protein is methylated at the glutamine residue in position 150 [Lhoest77, Arnold99]. A prmB mutant which lacks methylation of L3 has a cold-sensitive growth phenotype and accumulates abnormal ribosomal particles; however, lack of L3 methylation does not appear to affect ribosome function once the ribosome is assembled [Lhoest81].

L3 interacts with 23S rRNA [Uchiumi99]; this interaction appears to be cooperative with L6 [Uchiumi99].

An L3 mutant strain is resistant to the antibiotics tiamulin (a peptidyl transferase inhibitor) and pleuromutilin, but not valnemulin [Bosling03, Long06]. An amber mutation in rplC exerts a polar effect on the genes distal to the rplC gene in the S10 operon [Cabezon80].

Gene Citations: [Zurawski85]

Locations: cytosol, ribosome

Map Position: [3,450,319 <- 3,450,948] (74.37 centisomes, 268°)
Length: 630 bp / 209 aa

Molecular Weight of Polypeptide: 22.243 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0010860, CGSC:261, DIP:DIP-10744N, EchoBASE:EB0859, EcoGene:EG10866, EcoliWiki:b3320, Mint:MINT-1302843, ModBase:P60438, OU-Microarray:b3320, PortEco:rplC, PR:PRO_000023811, Pride:P60438, Protein Model Portal:P60438, RefSeq:NP_417779, RegulonDB:EG10866, SMR:P60438, String:511145.b3320, UniProt:P60438

Relationship Links: InterPro:IN-FAMILY:IPR000597, InterPro:IN-FAMILY:IPR009000, InterPro:IN-FAMILY:IPR019926, InterPro:IN-FAMILY:IPR019927, Panther:IN-FAMILY:PTHR11229, PDB:Structure:1ML5, PDB:Structure:2J28, PDB:Structure:2RDO, PDB:Structure:3BBX, PDB:Structure:3J5L, PDB:Structure:3J7Z, PDB:Structure:3J9Y, PDB:Structure:4CSU, PDB:Structure:4U1U, PDB:Structure:4U1V, PDB:Structure:4U20, PDB:Structure:4U24, PDB:Structure:4U25, PDB:Structure:4U26, PDB:Structure:4U27, PDB:Structure:4UY8, PDB:Structure:4V6E, PDB:Structure:4V6K, PDB:Structure:4V6L, PDB:Structure:4V6M, PDB:Structure:4V6N, PDB:Structure:4V6O, PDB:Structure:4V6P, PDB:Structure:4V6Q, PDB:Structure:4V6R, PDB:Structure:4V6S, PDB:Structure:4V6T, PDB:Structure:4V6V, PDB:Structure:4V6Y, PDB:Structure:4V6Z, PDB:Structure:4V7V, PDB:Structure:4V9C, PDB:Structure:4V9D, PDB:Structure:4V9O, PDB:Structure:4V9P, PDB:Structure:4V47, PDB:Structure:4V48, PDB:Structure:4V4H, PDB:Structure:4V4Q, PDB:Structure:4V4V, PDB:Structure:4V4W, PDB:Structure:4V50, PDB:Structure:4V52, PDB:Structure:4V53, PDB:Structure:4V54, PDB:Structure:4V55, PDB:Structure:4V56, PDB:Structure:4V57, PDB:Structure:4V5B, PDB:Structure:4V5H, PDB:Structure:4V5Y, PDB:Structure:4V64, PDB:Structure:4V65, PDB:Structure:4V66, PDB:Structure:4V69, PDB:Structure:4V6C, PDB:Structure:4V6D, PDB:Structure:4V70, PDB:Structure:4V71, PDB:Structure:4V72, PDB:Structure:4V73, PDB:Structure:4V74, PDB:Structure:4V75, PDB:Structure:4V76, PDB:Structure:4V77, PDB:Structure:4V78, PDB:Structure:4V79, PDB:Structure:4V7A, PDB:Structure:4V7B, PDB:Structure:4V7C, PDB:Structure:4V7D, PDB:Structure:4V7I, PDB:Structure:4V7S, PDB:Structure:4V7T, PDB:Structure:4V7U, PDB:Structure:4V85, PDB:Structure:4V89, PDB:Structure:4WF1, PDB:Structure:4WWW, PDB:Structure:4YBB, PDB:Structure:5AFI, PDB:Structure:5AKA, Pfam:IN-FAMILY:PF00297, Prosite:IN-FAMILY:PS00474

Gene-Reaction Schematic

Gene-Reaction Schematic

Genetic Regulation Schematic

Genetic regulation schematic for rplC


GO Terms:
Biological Process:
Inferred by computational analysisGO:0006412 - translation [GOA06, GOA01a]
Molecular Function:
Inferred from experimentGO:0005515 - protein binding [Zheng11]
Inferred by computational analysisGO:0003723 - RNA binding [UniProtGOA11a]
Inferred by computational analysisGO:0003735 - structural constituent of ribosome [GOA01a]
Inferred by computational analysisGO:0019843 - rRNA binding [UniProtGOA11a, GOA06]
Cellular Component:
Inferred from experimentInferred by computational analysisGO:0005829 - cytosol [DiazMejia09, Ishihama08]
Inferred from experimentGO:0022625 - cytosolic large ribosomal subunit [Hindennach71]
Inferred by computational analysisGO:0005840 - ribosome [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0030529 - ribonucleoprotein complex [UniProtGOA11a]

MultiFun Terms: cell structureribosomes
information transferprotein relatedribosomal proteins
information transferprotein relatedtranslation

Essentiality data for rplC knockouts:

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

Credits:
Last-Curated 31-Mar-2006 by Keseler I, SRI International


Subunit of: 50S ribosomal subunit

Inferred from experiment

Synonyms: ribosome, large subunit

Subunit composition of 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 (extended 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 (extended 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 (extended 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 (extended summary available)

Component of: ribosome (summary available)

Relationship Links: PDB:Structure:1P85, PDB:Structure:1P86, PDB:Structure:2AW4, PDB:Structure:2AWB

Credits:
Created 02-Jun-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 (extended 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 (extended 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 (extended 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 (extended 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 [Zhang09, 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, Goldman15]

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

Enzymes activated by ribosome, sorted by the type of activation, are:

Activator (Mechanism unknown) of: ATPase [Becker12]

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


Sequence Features

Protein sequence of 50S ribosomal subunit protein L3 with features indicated

Feature Class Location Citations Comment State
Pfam PF00297 27 -> 182
Inferred by computational analysis[Finn14]
Ribosomal_L3 : Ribosomal protein L3
 
N6-succinyllysine-Modification 38
Inferred from experiment[Zhang11b]
UniProt: N6-succinyllysine.
 
Methylation-Modification 150
Inferred from experiment[Muranova78, Muranova78, Lhoest77, Arnold99]
  Modified


Gene Local Context (not to scale -- see Genome Browser for correct scale)

Gene local context diagram

Transcription Unit

Transcription-unit diagram

Notes:

History:
10/20/97 Gene b3320 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10866; confirmed by SwissProt match.


References

Arnold99: Arnold RJ, Reilly JP (1999). "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry." Anal Biochem 269(1);105-12. PMID: 10094780

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

Becker12: Becker M, Gzyl KE, Altamirano AM, Vuong A, Urban K, Wieden HJ (2012). "The 70S ribosome modulates the ATPase activity of Escherichia coli YchF." RNA Biol 9(10);1288-301. PMID: 22995830

Bosling03: Bosling J, Poulsen SM, Vester B, Long KS (2003). "Resistance to the peptidyl transferase inhibitor tiamulin caused by mutation of ribosomal protein l3." Antimicrob Agents Chemother 47(9);2892-6. PMID: 12936991

Cabezon80: Cabezon T, Delcuve G, Faelen M, Desmet L, Bollen A (1980). "Polarity of amber mutations in ribosomal protein genes of Escherichia coli." J Bacteriol 141(1);41-51. PMID: 6986365

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

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

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."

Goldman15: Goldman DH, Kaiser CM, Milin A, Righini M, Tinoco I, Bustamante C (2015). "Ribosome. Mechanical force releases nascent chain-mediated ribosome arrest in vitro and in vivo." Science 348(6233);457-60. PMID: 25908824

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

Hindennach71: Hindennach I, Kaltschmidt E, Wittmann HG (1971). "Ribosomal proteins. Isolation of proteins from 50S ribosomal subunits of Escherichia coli." Eur J Biochem 23(1);12-6. PMID: 4942547

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

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

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

Lhoest77: Lhoest J, Colson C (1977). "Genetics of ribosomal protein methylation in Escherichia coli. II. A mutant lacking a new type of methylated amino acid, N5-methylglutamine, in protein L3." Mol Gen Genet 154(2);175-80. PMID: 331083

Lhoest81: Lhoest J, Colson C (1981). "Cold-sensitive ribosome assembly in an Escherichia coli mutant lacking a single methyl group in ribosomal protein L3." Eur J Biochem 121(1);33-7. PMID: 6173216

Long06: Long KS, Hansen LH, Jakobsen L, Vester B (2006). "Interaction of pleuromutilin derivatives with the ribosomal peptidyl transferase center." Antimicrob Agents Chemother 50(4);1458-62. PMID: 16569865

Muranova78: Muranova TA, Muranov AV, Markova LF, Ovchinnikov YA (1978). "The primary structure of ribosomal protein L3 from Escherichia coli 70 S ribosomes." FEBS Lett 96(2);301-5. PMID: 365579

Nowotny82: Nowotny V, Nierhaus KH (1982). "Initiator proteins for the assembly of the 50S subunit from Escherichia coli ribosomes." Proc Natl Acad Sci U S A 79(23);7238-42. PMID: 6760192

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

Olins81: Olins PO, Nomura M (1981). "Regulation of the S10 ribosomal protein operon in E. coli: nucleotide sequence at the start of the operon." Cell 1981;26(2 Pt 2);205-11. PMID: 7037196

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

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

Uchiumi99: Uchiumi T, Sato N, Wada A, Hachimori A (1999). "Interaction of the sarcin/ricin domain of 23 S ribosomal RNA with proteins L3 and L6." J Biol Chem 274(2);681-6. PMID: 9873002

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

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

Zhang09: Zhang W, Dunkle JA, Cate JH (2009). "Structures of the ribosome in intermediate states of ratcheting." Science 325(5943);1014-7. PMID: 19696352

Zhang11b: Zhang Z, Tan M, Xie Z, Dai L, Chen Y, Zhao Y (2011). "Identification of lysine succinylation as a new post-translational modification." Nat Chem Biol 7(1);58-63. PMID: 21151122

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

Zurawski85: Zurawski G, Zurawski SM (1985). "Structure of the Escherichia coli S10 ribosomal protein operon." Nucleic Acids Res 1985;13(12);4521-6. PMID: 3892488

Other References Related to Gene Regulation

Cerretti83: Cerretti DP, Dean D, Davis GR, Bedwell DM, Nomura M (1983). "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene." Nucleic Acids Res 1983;11(9);2599-616. PMID: 6222285

Lemke11: Lemke JJ, Sanchez-Vazquez P, Burgos HL, Hedberg G, Ross W, Gourse RL (2011). "Direct regulation of Escherichia coli ribosomal protein promoters by the transcription factors ppGpp and DksA." Proc Natl Acad Sci U S A 108(14);5712-7. PMID: 21402902

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Salmon05: Salmon KA, Hung SP, Steffen NR, Krupp R, Baldi P, Hatfield GW, Gunsalus RP (2005). "Global gene expression profiling in Escherichia coli K12: effects of oxygen availability and ArcA." J Biol Chem 280(15);15084-96. PMID: 15699038

Sha95: Sha Y, Lindahl L, Zengel JM (1995). "Role of NusA in L4-mediated attenuation control of the S10 r-protein operon of Escherichia coli." J Mol Biol 245(5);474-85. PMID: 7844821


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Sat Feb 13, 2016, biocyc14.