Publication Date:
1999-03-26
Description:
The carboxyl-terminal domain of colicin E5 was shown to inhibit protein synthesis of Escherichia coli. Its target, as revealed through in vivo and in vitro experiments, was not ribosomes as in the case of E3, but the transfer RNAs (tRNAs) for Tyr, His, Asn, and Asp, which contain a modified base, queuine, at the wobble position of each anticodon. The E5 carboxyl-terminal domain hydrolyzed these tRNAs just on the 3' side of this nucleotide. Tight correlation was observed between the toxicity of E5 and the cleavage of intracellular tRNAs of this group, implying that these tRNAs are the primary targets of colicin E5.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogawa, T -- Tomita, K -- Ueda, T -- Watanabe, K -- Uozumi, T -- Masaki, H -- New York, N.Y. -- Science. 1999 Mar 26;283(5410):2097-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biotechnology, Graduate School of Agricultural and Life Sciences, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10092236" target="_blank"〉PubMed〈/a〉
Keywords:
Anticodon/*metabolism
;
Bacterial Proteins/biosynthesis/genetics/pharmacology
;
Base Sequence
;
Cloning, Molecular
;
Colicins/genetics/*metabolism/pharmacology
;
Escherichia coli/drug effects/metabolism
;
*Escherichia coli Proteins
;
Guanine/analogs & derivatives/analysis
;
Molecular Sequence Data
;
RNA, Bacterial/chemistry/*metabolism
;
RNA, Ribosomal, 16S/metabolism
;
RNA, Transfer, Amino Acid-Specific/chemistry/*metabolism
;
RNA, Transfer, Asn/chemistry/metabolism
;
RNA, Transfer, Asp/chemistry/metabolism
;
RNA, Transfer, His/chemistry/metabolism
;
RNA, Transfer, Tyr/chemistry/metabolism
;
Ribonucleases/genetics/*metabolism/pharmacology
;
Ribosomes/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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