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Escherichia coli K-12 substr. MG1655 Polypeptide: 50S ribosomal subunit protein L2



Gene: rplB Accession Numbers: EG10865 (EcoCyc), b3317, ECK3304

Regulation Summary Diagram: ?

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

Summary:
The L2 protein is a component of the 50S subunit of the ribosome and is part of the peptidyltransferase center. L2 is highly evolutionarily conserved [Schmid84, Uhlein98].

L2 is required for the association of the 30S and 50S subunits [Diedrich00]; one end of the elongated L2 protein is located at the intersubunit interface of the 50S subunit [Willumeit01]. L2 is involved in binding of tRNA to both the A and P sites, and the His229 residue appears to be important for peptidyl-transferase activity of the ribosome [Diedrich00]. A conserved region within L2 is required for assembly of L16 into the 50S ribosomal subunit [Romero90]. Ribosome modulation factor binds near L2, L13, and S13 [Yoshida02a].

L2 interacts with domains II and IV of 23S rRNA [Egebjerg91, Beauclerk88, Thiede98, Ostergaard98] and with 5S rRNA [Okada00]. L2 also interacts with aminoacyl-tRNA [Metspalu81, Remme85, Sumpter90].

Gene Citations: [Zurawski85]

Locations: cytosol, ribosome

Map Position: [3,448,565 <- 3,449,386] (74.33 centisomes)
Length: 822 bp / 273 aa

Molecular Weight of Polypeptide: 29.86 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0010854 , CGSC:262 , DIP:DIP-35747N , EchoBASE:EB0858 , EcoGene:EG10865 , EcoliWiki:b3317 , Mint:MINT-1322809 , ModBase:P60422 , OU-Microarray:b3317 , PortEco:rplB , PR:PRO_000023810 , Pride:P60422 , Protein Model Portal:P60422 , RefSeq:NP_417776 , RegulonDB:EG10865 , SMR:P60422 , String:511145.b3317 , UniProt:P60422

Relationship Links: InterPro:IN-FAMILY:IPR002171 , InterPro:IN-FAMILY:IPR005880 , InterPro:IN-FAMILY:IPR008991 , InterPro:IN-FAMILY:IPR012340 , InterPro:IN-FAMILY:IPR014722 , InterPro:IN-FAMILY:IPR014726 , InterPro:IN-FAMILY:IPR022666 , InterPro:IN-FAMILY:IPR022669 , InterPro:IN-FAMILY:IPR022671 , Panther:IN-FAMILY:PTHR13691 , Panther:IN-FAMILY:PTHR13691:SF5 , PDB:Structure:1P85 , PDB:Structure:1P86 , PDB:Structure:1VS6 , PDB:Structure:1VS8 , PDB:Structure:1VT2 , PDB:Structure:2AW4 , PDB:Structure:2AWB , PDB:Structure:2GYA , PDB:Structure:2GYC , PDB:Structure:2I2T , PDB:Structure:2I2V , PDB:Structure:2J28 , PDB:Structure:2QAM , PDB:Structure:2QAO , PDB:Structure:2QBA , PDB:Structure:2QBC , PDB:Structure:2QBE , PDB:Structure:2QBG , PDB:Structure:2QBI , PDB:Structure:2QBK , PDB:Structure:2QOV , PDB:Structure:2QOX , PDB:Structure:2QOZ , PDB:Structure:2QP1 , PDB:Structure:2RDO , PDB:Structure:2VHM , PDB:Structure:2VHN , PDB:Structure:2WWQ , PDB:Structure:2Z4L , PDB:Structure:2Z4N , PDB:Structure:3BBX , PDB:Structure:3DF2 , PDB:Structure:3DF4 , PDB:Structure:3E1B , PDB:Structure:3E1D , PDB:Structure:3FIK , PDB:Structure:3I1N , PDB:Structure:3I1P , PDB:Structure:3I1R , PDB:Structure:3I1T , PDB:Structure:3I20 , PDB:Structure:3I22 , PDB:Structure:3IZT , PDB:Structure:3IZU , PDB:Structure:3J01 , PDB:Structure:3J0T , PDB:Structure:3J0W , PDB:Structure:3J0Y , PDB:Structure:3J11 , PDB:Structure:3J12 , PDB:Structure:3J14 , PDB:Structure:3J19 , PDB:Structure:3J37 , PDB:Structure:3KCR , PDB:Structure:3OAS , PDB:Structure:3OAT , PDB:Structure:3OFC , PDB:Structure:3OFD , PDB:Structure:3OFQ , PDB:Structure:3OFR , PDB:Structure:3OFZ , PDB:Structure:3OG0 , PDB:Structure:3ORB , PDB:Structure:3R8S , PDB:Structure:3R8T , PDB:Structure:3SGF , PDB:Structure:3UOS , PDB:Structure:487D , PDB:Structure:4GAR , PDB:Structure:4GAU , PDB:Structure:4KIX , PDB:Structure:4KIZ , PDB:Structure:4KJ1 , PDB:Structure:4KJ3 , PDB:Structure:4KJ5 , PDB:Structure:4KJ7 , PDB:Structure:4KJ9 , PDB:Structure:4KJB , Pfam:IN-FAMILY:PF00181 , Pfam:IN-FAMILY:PF03947 , Prosite:IN-FAMILY:PS00467

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 [Rajagopala14, Chodavarapu11, Rippa10a, Arifuzzaman06, Butland05]
GO:0008270 - zinc ion binding Inferred from experiment [Katayama02]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0003735 - structural constituent of ribosome Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [GOA01]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11, GOA06]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Ishihama08, Zhang07]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a]
GO:0005622 - intracellular Inferred by computational analysis [GOA01]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0015934 - large ribosomal subunit Inferred by computational analysis [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 rplB 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 ? 30-Mar-2006 by Keseler I , SRI International


Subunit of: 50S ribosomal subunit

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 (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)

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 (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 [Zhang09b, 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
Cleavage-of-Initial-Methionine 1
[Kimura82, UniProt12a]
UniProt: Removed.
Chain 2 -> 273
[UniProt09]
UniProt: 50S ribosomal protein L2;
Mutagenesis-Variant 230
[Diedrich00, Cooperman, UniProt11]
Alternate sequence: H → Q; UniProt: Loss of peptidyltransferase activity in reconstituted ribosomes. No change in rRNA binding or assembly into ribosomes.
Sequence-Conflict 232 -> 235
[Kimura82, UniProt10a]
Alternate sequence: HGGG → GGGH; UniProt: (in Ref. 4; AA sequence);
Acetylation-Modification 242
[Zhang09, UniProt11]
UniProt: N6-acetyllysine.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b3317 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10865; confirmed by SwissProt match.


References

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

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

Beauclerk88: Beauclerk AA, Cundliffe E (1988). "The binding site for ribosomal protein L2 within 23S ribosomal RNA of Escherichia coli." EMBO J 7(11);3589-94. PMID: 3061801

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Chodavarapu11: Chodavarapu S, Felczak MM, Kaguni JM (2011). "Two forms of ribosomal protein L2 of Escherichia coli that inhibit DnaA in DNA replication." Nucleic Acids Res 39(10);4180-91. PMID: 21288885

Cooperman: Cooperman BS, Wooten T, Romero DP, Traut RR "Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity." Biochem Cell Biol 73(11-12);1087-94. PMID: 8722025

Diedrich00: Diedrich G, Spahn CM, Stelzl U, Schafer MA, Wooten T, Bochkariov DE, Cooperman BS, Traut RR, Nierhaus KH (2000). "Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer." EMBO J 19(19);5241-50. PMID: 11013226

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

Egebjerg91: Egebjerg J, Christiansen J, Garrett RA (1991). "Attachment sites of primary binding proteins L1, L2 and L23 on 23 S ribosomal RNA of Escherichia coli." J Mol Biol 222(2);251-64. PMID: 1960726

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."

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

Hindennach71a: 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

Katayama02: Katayama A, Tsujii A, Wada A, Nishino T, Ishihama A (2002). "Systematic search for zinc-binding proteins in Escherichia coli." Eur J Biochem 269(9);2403-13. PMID: 11985624

Kimura82: Kimura M., Mende L., Wittmann-Liebold B. (1982). "The primary structure of protein L2 from the Escherichia coli ribosome." FEBS Lett., Volume 149, page(s) 304-312.

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

Metspalu81: Metspalu E, Maimets T, Ustav M, Villems R (1981). "A quaternary complex consisting of two molecules of tRNA and ribosomal proteins L2 and L17." FEBS Lett 132(1);105-8. PMID: 6170527

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

Okada00: Okada S, Okada T, Aimi T, Morinaga T, Itoh T (2000). "HSP70 and ribosomal protein L2: novel 5S rRNA binding proteins in Escherichia coli." FEBS Lett 485(2-3);153-6. PMID: 11094158

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

Ostergaard98: Ostergaard P, Phan H, Johansen LB, Egebjerg J, Ostergaard L, Porse BT, Garrett RA (1998). "Assembly of proteins and 5 S rRNA to transcripts of the major structural domains of 23 S rRNA." J Mol Biol 284(2);227-40. PMID: 9813114

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

Remme85: Remme J, Metspalu E, Maimets T, Villems R (1985). "The properties of the complex between ribosomal protein L2 and tRNA." FEBS Lett 190(2);275-8. PMID: 2412896

Rippa10a: Rippa V, Cirulli C, Di Palo B, Doti N, Amoresano A, Duilio A (2010). "The ribosomal protein L2 interacts with the RNA polymerase alpha subunit and acts as a transcription modulator in Escherichia coli." J Bacteriol 192(7);1882-9. PMID: 20097853

Romero90: Romero DP, Arredondo JA, Traut RR (1990). "Identification of a region of Escherichia coli ribosomal protein L2 required for the assembly of L16 into the 50 S ribosomal subunit." J Biol Chem 265(30);18185-91. PMID: 2211695

Schmid84: Schmid G, Strobel O, Stoffler-Meilicke M, Stoffler G, Bock A (1984). "A ribosomal protein that is immunologically conserved in archaebacteria, eubacteria and eukaryotes." FEBS Lett 177(2);189-94. PMID: 6209167

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

Sumpter90: Sumpter VG, Tate WP, Nierhaus KH (1990). "The complex between ribosomal proteins and aminoacyl-tRNA: the interactions and hydrolytic activities are not confined to the proteins L2 and L16 of Escherichia coli ribosomes." Biochim Biophys Acta 1048(2-3);265-9. PMID: 2182127

Thiede98: Thiede B, Urlaub H, Neubauer H, Grelle G, Wittmann-Liebold B (1998). "Precise determination of RNA-protein contact sites in the 50 S ribosomal subunit of Escherichia coli." Biochem J 334 ( Pt 1);39-42. PMID: 9693099

Uhlein98: Uhlein M, Weglohner W, Urlaub H, Wittmann-Liebold B (1998). "Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies." Biochem J 331 ( Pt 2);423-30. PMID: 9531480

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

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.

UniProt12a: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 00:00:00." Database.

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

Willumeit01: Willumeit R, Forthmann S, Beckmann J, Diedrich G, Ratering R, Stuhrmann HB, Nierhaus KH (2001). "Localization of the protein L2 in the 50 S subunit and the 70 S E. coli ribosome." J Mol Biol 305(1);167-77. PMID: 11114255

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

Yoshida02a: Yoshida H, Maki Y, Kato H, Fujisawa H, Izutsu K, Wada C, Wada A (2002). "The ribosome modulation factor (RMF) binding site on the 100S ribosome of Escherichia coli." J Biochem (Tokyo) 132(6);983-9. PMID: 12473202

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

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

Zhang09b: Zhang W, Dunkle JA, Cate JH (2009). "Structures of the ribosome in intermediate states of ratcheting." Science 325(5943);1014-7. PMID: 19696352

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


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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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