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PMID: 3881393 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Antisuppressor mutation in Escherichia coli defective in biosynthesis of 5-methylaminomethyl-2-thiouridine.

Journal of bacteriology ·Vol. 161 ·No. 1 ·1985-01-00 ·Pages 368-76

Sullivan MA, Cannon JF, Webb FH, Bock RM

Abstract

Mutations in three Escherichia coli K-12 genes were isolated that reduce the efficiency of the lysine-inserting nonsense suppressor supL. These antisuppressor mutations asuD, asuE, and asuF map at 61.9, 25.3, and 76.3 min, respectively, on the E. coli chromosome. Biochemical and genetic analysis of the mutant strains revealed the reason for the antisuppressor phenotype for two of these genes. The activity of lysyl-tRNA synthetase was reduced in strains with asuD mutations. The modification of 5-methylaminomethyl-2-thiouridine, the wobble base of tRNALys, was impaired in asuE mutant strains, presumably at the 2-thiolation step.

MeSH Terms
Chromosome Mapping Chromosomes, Bacterial Escherichia coli/genetics Lysine-tRNA Ligase/metabolism Plasmids RNA, Transfer, Amino Acyl/metabolism Suppression, Genetic Thiouridine/analogs & derivatives,genetics Transduction, Genetic
Chemicals
RNA, Transfer, Amino Acyl Thiouridine 5-methylaminomethyl-2-thiouridine Lysine-tRNA Ligase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sullivan M A
Cannon J F
Webb F H
Bock R M
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.161.1.368-376.1985
Published
1985-01-00
Pages
368-76
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC214881
Subset
IM
Grants
NIGMS NIH HHS · GM 07215 · United States
External Links
PubMed source DOI: 10.1128/jb.161.1.368-376.1985 PMC Full Text View journal details
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