Ribosomal protein L7/L12 is required for optimal translation.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 77 ·No. 7 ·1980-07-00 ·Pages 4007-10

Pettersson I, Kurland CG

Abstract

We have tested the performance in vitro of Escherichia coli ribosomes containing or lacking the protein L7/L12. When the experiments are performed in an optimized mixture of ions (polymix), L7/L12 is required for maximal rate of synthesis as well as for minimal missense error frequency. The results in conventional Tris/Mg2+/NH4Cl buffers are different; in these buffers, only the rate of synthesis is strongly dependent on the presence of L7/L12. In addition, we show that there is a large difference between the optimal Mg2+ concentration required for speed of translation and that for accuracy of translation in conventional buffer. These optima are very close in polymix. Finally, we show that the contribution of L7/L12 to the speed of translation is obscured in translation systems that are limited by substrates. We conclude that it is not possible to analyze details of the mechanism of translation in conventional buffers.

MeSH Terms

Bacterial Proteins/genetics Escherichia coli Kinetics Magnesium/metabolism Osmolar Concentration Protein Biosynthesis RNA, Transfer, Amino Acyl/metabolism Ribosomal Proteins/genetics Ribosomes/metabolism Structure-Activity Relationship

Chemicals

Bacterial Proteins RNA, Transfer, Amino Acyl Ribosomal Proteins Magnesium

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Pettersson I

Kurland C G

References (26)

26 references, click to expand

Elongation factor-dependent reactions of ribosomes deprived of proteins L7 and L12.
FEBS Lett. 1977 Jan 15;73(1):6-11 PMID: 320039
Reconstitution of a GTPase activity by a 50S ribosomal protein and E. coli.
Nat New Biol. 1971 Sep 8;233(36):62-3 PMID: 4329351
Small-angle X-ray scattering and crosslinking study of the proteins L7/L12 from Escherichia coli ribosomes.
FEBS Lett. 1976 Jul 1;66(1):48-51 PMID: 776697
Dependence of initiation factor IF-2 activity on proteins L7 and L12 from Escherichia coli 50 S ribosomes.
J Biol Chem. 1973 Dec 25;248(24):8555-9 PMID: 4587128
The properties of an E. coli ribosomal protein required for the function of factor G.
Arch Biochem Biophys. 1972 Jan;148(1):148-55 PMID: 4550866
The role of ribosomal proteins L7 and L-12 in polypeptide chain initiation in Escherichia coli.
J Biol Chem. 1974 Feb 25;249(4):1213-8 PMID: 4360682
Studies on the ribosomal sites involved in factors Tu and G-dependent reactions.
Arch Biochem Biophys. 1972 Mar;149(1):110-7 PMID: 4552797
The stoichiometry of the ribosomal proteins of Escherichia coli.
Mol Gen Genet. 1975 Oct 3;140(3):253-74 PMID: 1107798
Effect of ribosomal protein L12 upon initiation factor IF-2 activities.
Biochem Biophys Res Commun. 1973 Apr 16;51(4):979-86 PMID: 4350001
Studies on the role of ribosomal proteins L 7 and L 12 in the in vitro synthesis of -galactosidase.
J Biol Chem. 1973 Jul 25;248(14):5012-5 PMID: 4352186
Further studies on the role of 50 S ribosomal proteins in protein synthesis.
J Biol Chem. 1973 Oct 25;248(20):6952-6 PMID: 4582729
Isolation and characterization of two acidic proteins from the 50S subunit required for GTPase activities of both EF G and EF T.
Biochem Biophys Res Commun. 1972 May 26;47(4):866-73 PMID: 4337326
Components of the 50S ribosomal subunit involved in GTP cleavage.
Biochem Biophys Res Commun. 1972 Jan 14;46(1):238-44 PMID: 4550081
Structural and functional evidence for a repeated 50S subunit ribosomal protein.
Nat New Biol. 1973 Mar 14;242(115):47-9 PMID: 4571811
The dependence of cell-free protein synthesis in E. coli upon naturally occurring or synthetic polyribonucleotides.
Proc Natl Acad Sci U S A. 1961 Oct 15;47:1588-602 PMID: 14479932
The stoichiometry and reconstitution of a stable protein complex from Escherichia coli ribosomes.
FEBS Lett. 1979 Feb 1;98(1):139-44 PMID: 371980
Polypeptide chain elongation in protein biosynthesis.
Science. 1969 May 30;164(3883):1024-31 PMID: 4890174
The effect of enzymatically synthesized ribonucleic acid on amino acid incorporation by a soluble protein-ribosome system from Escherichia coli.
Proc Natl Acad Sci U S A. 1962 Jan 15;48:94-104 PMID: 14040327
The primary structure of an acidic protein from 50-S ribosomes of Escherichia coli which is involved in GTP hydrolysis dependent on elongation factors G and T.
Eur J Biochem. 1973 Apr 2;34(1):138-52 PMID: 4573678
The role of guanosine 5'-triphosphate in polypeptide chain elongation.
Biochim Biophys Acta. 1978 Sep 21;505(1):95-127 PMID: 361078
Nucleoside triphosphate regeneration decreases the frequency of translation errors.
Proc Natl Acad Sci U S A. 1979 Jul;76(7):3174-8 PMID: 290995
The role of Escherichia coli ribosomal proteins L7 and L12 in peptide chain propagation.
FEBS Lett. 1977 Jan 15;73(1):1-5 PMID: 320033
50-S ribosomal proteins. Purification and partial characterization of two acidic proteins, A 1 and A 2, isolated from 50-S ribosomes of Escherichia coli.
Eur J Biochem. 1972 Jan 31;25(1):5-12 PMID: 4554105
Requirement of an Escherichia coli 50 S ribosomal protein component for effective interaction of the ribosome with T and G factors and with guanosine triphosphate.
J Biol Chem. 1972 Feb 10;247(3):805-14 PMID: 4333515
A procedure for isolation of spontaneous mutants with temperature sensitive of RNA and/or protein.
Mol Gen Genet. 1977 Nov 18;156(3):233-7 PMID: 340905
Copies of proteins L7 and L12 and heterogeneity of the large subunit of Escherichia coli ribosome.
J Mol Biol. 1975 Jun 15;95(1):1-8 PMID: 1097708

Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.77.7.4007

Published

1980-07-00

Pages

4007-10

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC349757

Subset

External Links

PubMed source DOI: 10.1073/pnas.77.7.4007 PMC Full Text View journal details

Analysis Services

Ribosomal protein L7/L12 is required for optimal translation.

Contact

WeChat Official Account