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PMID: 775446 Published · ppublish English Journal Article

Patterns of E. coli leucine tRNA isoacceptors following bacteriophage MS2 infection.

Nucleic acids research ·Vol. 3 ·No. 4 ·1976-04-00 ·Pages 917-30

Di Natale P, Eilat D

Abstract

The RNA extracted from MS2 phage particles can accept radioactive leucine and serine in the presence of tRNA activating enzymes. Leucine acceptance is due to the presence of E. coli leucine tRNA that binds very tightly to the virus particle. RPC-5 column chromatography shows that the pattern of virus associated leucyl-tRNA isoacceptors is different from that of normal E. coli leucyl-tRNA. It is also different from the pattern of host leucyl-tRNA isoacceptors found in E. coli lysate following MS2 phage infection. The RPC-5 pattern of the latter tRNA shows several new peaks of leucine tRNA isoacceptors. The possibility that these tRNAs are some modified forms of normal leucine tRNA isoacceptors is suggested.

MeSH Terms
Amino Acids/analysis Amino Acyl-tRNA Synthetases/metabolism Binding Sites Codon Coliphages/metabolism Escherichia coli/metabolism Leucine/metabolism RNA, Bacterial/metabolism RNA, Transfer/metabolism Ribosomes/metabolism Serine/metabolism Structure-Activity Relationship
Chemicals
Amino Acids Codon RNA, Bacterial Serine RNA, Transfer Amino Acyl-tRNA Synthetases Leucine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Di Natale P
Eilat D
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33 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/3.4.917
Published
1976-04-00
Pages
917-30
Language
English
Region
England
NLM ID
0411011
PMCID
PMC342955
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/3.4.917 PMC Full Text View journal details
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