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Escherichia coli K-12 substr. MG1655 Polypeptide: 50S ribosomal subunit protein L20



Gene: rplT Accession Numbers: EG10881 (EcoCyc), b1716, ECK1714

Synonyms: pdzA

Regulation Summary Diagram: ?

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

Summary:
The L20 protein is a component of the 50S subunit of the ribosome and autoregulates its own expression and that of L35 at the posttranscriptional level. The N-terminal domain of L20 is required for ribosome assembly, and the C-terminal domain is required for its regulatory function [Guillier05].

L20 binds to the 5' terminal third of 23S rRNA [Spierer75, Marquardt79, Tumminia94] and is required for early assembly of the 4.3c core particle, but is not required for function of the mature 50S ribosomal subunit [Nowotny80]. L20 can replace L24 for the initiation of assembly of the 50S subunit at permissive temperatures in an L24 mutant [Franceschi88]. L20 can be crosslinked to L13 and L21 [Walleczek89, Redl89, Walleczek89a].

L20 might be required for maintaining the 50S subunit in the correct conformation for binding of aminoacyl-tRNAs [Kazemie76]. Decreasing the amount of L20 in the cell leads to a decrease in growth rate and the appearance of an aberrant ribosome peak at 41-43S [Olsson96].

Expression of rplT is autoregulated at the posttranscriptional level. L20 acts in trans at two sites, one located within infC [Lesage90] and a second located close to the translation start site of rpmI [Chiaruttini96]. The two sites may form a long-range RNA pseudoknot structure [Chiaruttini96]. Of the two L20 binding sites within the regulatory region of the mRNA, only one shows direct similarity to the L20 binding site within 23S rRNA [Guillier02]. However, both sites share secondary structure similarity with the L20 binding site in rRNA [Guillier05a]. The two binding sites interact, and only one molecule of L20 binds to the L20 mRNA [Allemand07]. Structural analysis of RNA binding by the L20 C-terminal domain by NMR show that binding of L20 to rRNA and mRNA is similar [Raibaud03]. Decreased translation of infC leads to increased L20-mediated repression of L35 expression [Chiaruttini97].

L20 directly represses the expression of rpmI, but only indirectly that of rplT, via translational coupling with rpmI [Lesage92]. A secondary structure forms between the translation initiation site of rplT and a site internal to rpmI [Lesage92]; this structure forms in vivo and is required for translational coupling [Chiaruttini96a]. It is thought that the secondary structure can form when rpmI is not translated, and it can be shown that it blocks binding of the ribosome to the ribosome binding site of rplT [Chiaruttini96a].

Unlike the regulation of the ribosomal alpha operon and of rpsO, translational autoregulation by L20 appears to be based on competition with the ribosome for binding to its mRNA [HaentjensSitri08].

Gene Citations: [Fayat83, Wertheimer88, Wu84]

Locations: cytosol, ribosome

Map Position: [1,797,417 <- 1,797,773] (38.74 centisomes)
Length: 357 bp / 118 aa

Molecular Weight of Polypeptide: 13.497 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0005729 , CGSC:17608 , DIP:DIP-47941N , EchoBASE:EB0874 , EcoGene:EG10881 , EcoliWiki:b1716 , Mint:MINT-1321645 , ModBase:P0A7L3 , OU-Microarray:b1716 , PortEco:rplT , PR:PRO_000023826 , Pride:P0A7L3 , Protein Model Portal:P0A7L3 , RefSeq:NP_416231 , RegulonDB:EG10881 , SMR:P0A7L3 , String:511145.b1716 , UniProt:P0A7L3

Relationship Links: InterPro:IN-FAMILY:IPR005813 , Panther:IN-FAMILY:PTHR10986 , 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: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:PF00453 , Prints:IN-FAMILY:PR00062 , Prosite:IN-FAMILY:PS00937

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0000027 - ribosomal large subunit assembly Inferred from experiment [Nowotny80]
GO:0006412 - translation Inferred from experiment Inferred by computational analysis [GOA01a]
GO:0017148 - negative regulation of translation Inferred from experiment [Lesage92]
Molecular Function: GO:0000900 - translation repressor activity, nucleic acid binding Inferred from experiment [Lesage92]
GO:0003735 - structural constituent of ribosome Inferred from experiment Inferred by computational analysis [GOA01a, Nowotny80]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0019843 - rRNA binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0022625 - cytosolic large ribosomal subunit Inferred from experiment [Hindennach71a, Olsson96]
GO:0005840 - ribosome Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0030529 - ribonucleoprotein complex Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure ribosomes
information transfer protein related ribosomal proteins
information transfer protein related translation
regulation type of regulation posttranscriptional

Essentiality data for rplT 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 ? 10-Jan-2008 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 [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]

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
[Hoving00, WittmannLiebold79]
 
Chain 2 -> 118
[UniProt09]
UniProt: 50S ribosomal protein L20;
Sequence-Conflict 33
[Fayat83, UniProt10]
Alternate sequence: R → A; UniProt: (in Ref. 1; CAA23562/AAA51468);


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b1716 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10881; confirmed by SwissProt match.


References

Allemand07: Allemand F, Haentjens J, Chiaruttini C, Royer C, Springer M (2007). "Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites." Nucleic Acids Res 35(9):3016-31. PMID: 17439971

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

Chiaruttini96: Chiaruttini C, Milet M, Springer M (1996). "A long-range RNA-RNA interaction forms a pseudoknot required for translational control of the IF3-L35-L20 ribosomal protein operon in Escherichia coli." EMBO J 15(16);4402-13. PMID: 8861967

Chiaruttini96a: Chiaruttini C, Milet M, de Smit M, Springer M (1996). "Translational coupling in the Escherichia coli operon encoding translation initiation factor IF3 and ribosomal proteins L20 and L35." Biochimie 78(7);555-67. PMID: 8955899

Chiaruttini97: Chiaruttini C, Milet M, Springer M (1997). "Translational coupling by modulation of feedback repression in the IF3 operon of Escherichia coli." Proc Natl Acad Sci U S A 94(17);9208-13. PMID: 9256461

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

Fayat83: Fayat G, Mayaux JF, Sacerdot C, Fromant M, Springer M, Grunberg-Manago M, Blanquet S (1983). "Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20." J Mol Biol 171(3);239-61. PMID: 6317865

Franceschi88: Franceschi FJ, Nierhaus KH (1988). "Ribosomal protein L20 can replace the assembly-initiator protein L24 at low temperatures." Biochemistry 27(18);7056-9. PMID: 2461735

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

Guillier02: Guillier M, Allemand F, Raibaud S, Dardel F, Springer M, Chiaruttini C (2002). "Translational feedback regulation of the gene for L35 in Escherichia coli requires binding of ribosomal protein L20 to two sites in its leader mRNA: a possible case of ribosomal RNA-messenger RNA molecular mimicry." RNA 8(7);878-89. PMID: 12166643

Guillier05: Guillier M, Allemand F, Graffe M, Raibaud S, Dardel F, Springer M, Chiaruttini C (2005). "The N-terminal extension of Escherichia coli ribosomal protein L20 is important for ribosome assembly, but dispensable for translational feedback control." RNA 11(5);728-38. PMID: 15840820

Guillier05a: Guillier M, Allemand F, Dardel F, Royer CA, Springer M, Chiaruttini C (2005). "Double molecular mimicry in Escherichia coli: binding of ribosomal protein L20 to its two sites in mRNA is similar to its binding to 23S rRNA." Mol Microbiol 56(6);1441-56. PMID: 15916597

HaentjensSitri08: Haentjens-Sitri J, Allemand F, Springer M, Chiaruttini C (2008). "A competition mechanism regulates the translation of the Escherichia coli operon encoding ribosomal proteins L35 and L20." J Mol Biol 375(3);612-25. PMID: 18037435

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

Hoving00: Hoving S, Munchbach M, Schmid H, Signor L, Lehmann A, Staudenmann W, Quadroni M, James P (2000). "A method for the chemical generation of N-terminal peptide sequence tags for rapid protein identification." Anal Chem 72(5);1006-14. PMID: 10739205

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

Kazemie76: Kazemie M (1976). "Binding of aminoacyl-tRNA to reconstituted subparticles of Escherichia coli large ribosomal subunits." Eur J Biochem 67(2);373-8. PMID: 786630

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

Lesage90: Lesage P, Truong HN, Graffe M, Dondon J, Springer M (1990). "Translated translational operator in Escherichia coli. Auto-regulation in the infC-rpmI-rplT operon." J Mol Biol 213(3);465-75. PMID: 2191140

Lesage92: Lesage P, Chiaruttini C, Graffe M, Dondon J, Milet M, Springer M (1992). "Messenger RNA secondary structure and translational coupling in the Escherichia coli operon encoding translation initiation factor IF3 and the ribosomal proteins, L35 and L20." J Mol Biol 228(2);366-86. PMID: 1453449

Marquardt79: Marquardt O, Roth HE, Wystup G, Nierhaus KH (1979). "Binding of Escherichia coli ribosomal proteins to 23S RNA under reconstitution conditions for the 50S subunit." Nucleic Acids Res 6(11);3641-50. PMID: 386275

Nowotny80: Nowotny V, Nierhaus KH (1980). "Protein L20 from the large subunit of Escherichia coli ribosomes is an assembly protein." J Mol Biol 137(4);391-9. PMID: 7021848

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

Olsson96: Olsson CL, Graffe M, Springer M, Hershey JW (1996). "Physiological effects of translation initiation factor IF3 and ribosomal protein L20 limitation in Escherichia coli." Mol Gen Genet 250(6);705-14. PMID: 8628231

Raibaud03: Raibaud S, Vachette P, Guillier M, Allemand F, Chiaruttini C, Dardel F (2003). "How bacterial ribosomal protein L20 assembles with 23 S ribosomal RNA and its own messenger RNA." J Biol Chem 278(38);36522-30. PMID: 12840018

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

Redl89: Redl B, Walleczek J, Stoffler-Meilicke M, Stoffler G (1989). "Immunoblotting analysis of protein-protein crosslinks within the 50S ribosomal subunit of Escherichia coli. A study using dimethylsuberimidate as crosslinking reagent." Eur J Biochem 181(2);351-6. PMID: 2653827

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

Spierer75: Spierer P, Zimmerman RA, Mackie GA (1975). "RNA-protein interactions in the ribosome. Binding of 50-S-subunit proteins to 5' and 3' terminal segments of the 23-S RNA." Eur J Biochem 52(3);459-68. PMID: 800986

Tumminia94: Tumminia SJ, Hellmann W, Wall JS, Boublik M (1994). "Visualization of protein-nucleic acid interactions involved in the in vitro assembly of the Escherichia coli 50 S ribosomal subunit." J Mol Biol 235(4);1239-50. PMID: 8308887

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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

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

Walleczek89: Walleczek J, Redl B, Stoffler-Meilicke M, Stoffler G (1989). "Protein-protein cross-linking of the 50 S ribosomal subunit of Escherichia coli using 2-iminothiolane. Identification of cross-links by immunoblotting techniques." J Biol Chem 264(7);4231-7. PMID: 2645289

Walleczek89a: Walleczek J, Martin T, Redl B, Stoffler-Meilicke M, Stoffler G (1989). "Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli." Biochemistry 28(9);4099-105. PMID: 2665813

Wertheimer88: Wertheimer SJ, Klotsky RA, Schwartz I (1988). "Transcriptional patterns for the thrS-infC-rplT operon of Escherichia coli." Gene 63(2);309-20. PMID: 2838394

WittmannLiebold79: Wittmann-Liebold B, Seib C (1979). "The primary structure of protein L20 from the large subunit of the Escherichia coli ribosome." FEBS Lett 103(1);61-5. PMID: 381019

Wu84: Wu TH, Wood DL, Stein PL, Comer MM (1984). "Transcription of a gene cluster coding for two aminoacyl-tRNA synthetases and an initiation factor in Escherichia coli." J Mol Biol 173(2);177-209. PMID: 6368838

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

Other References Related to Gene Regulation

Butler86: Butler JS, Springer M, Dondon J, Graffe M, Grunberg-Manago M (1986). "Escherichia coli protein synthesis initiation factor IF3 controls its own gene expression at the translational level in vivo." J Mol Biol 192(4);767-80. PMID: 2438418

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

Liveris91: Liveris D, Klotsky RA, Schwartz I (1991). "Growth rate regulation of translation initiation factor IF3 biosynthesis in Escherichia coli." J Bacteriol 173(12);3888-93. PMID: 2050639

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

Mayaux83: Mayaux JF, Fayat G, Fromant M, Springer M, Grunberg-Manago M, Blanquet S (1983). "Structural and transcriptional evidence for related thrS and infC expression." Proc Natl Acad Sci U S A 80(20);6152-6. PMID: 6353409

Partridge09: Partridge JD, Bodenmiller DM, Humphrys MS, Spiro S (2009). "NsrR targets in the Escherichia coli genome: new insights into DNA sequence requirements for binding and a role for NsrR in the regulation of motility." Mol Microbiol 73(4);680-94. PMID: 19656291

Pramanik86: Pramanik A, Wertheimer SJ, Schwartz JJ, Schwartz I (1986). "Expression of Escherichia coli infC: identification of a promoter in an upstream thrS coding sequence." J Bacteriol 168(2);746-51. PMID: 3536858

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

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

Springer86: Springer M, Graffe M, Butler JS, Grunberg-Manago M (1986). "Genetic definition of the translational operator of the threonine-tRNA ligase gene in Escherichia coli." Proc Natl Acad Sci U S A 83(12);4384-8. PMID: 3086882


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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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