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PMID: 2444436 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Bacteriophage T4 anticodon nuclease, polynucleotide kinase and RNA ligase reprocess the host lysine tRNA.

The EMBO journal ·Vol. 6 ·No. 8 ·1987-08-00 ·Pages 2499-503

Amitsur M, Levitz R, Kaufmann G

Abstract

Host tRNAs cleaved near the anticodon occur specifically in T4-infected Escherichia coli prr strains which restrict polynucleotide kinase (pnk) or RNA ligase (rli) phage mutants. The cleavage products are transient with wt but accumulate in pnk- or rli- infections, implicating the affected enzymes in repair of the damaged tRNAs. Their roles in the pathway were elucidated by comparing the mutant infection intermediates with intact tRNA counterparts before or late in wt infection. Thus, the T4-induced anticodon nuclease cleaves lysine tRNA 5' to the wobble position, yielding 2':3'-P greater than and 5'-OH termini. Polynucleotide kinase converts them into a 3'-OH and 5' P pair joined in turn by RNA ligase. Presumably, lysine tRNA depletion, in the absence of polynucleotide kinase and RNA ligase mediated repair, underlies prr restriction. However, the nuclease, kinase and ligase may benefit T4 directly, by adapting levels or decoding specificities of host tRNAs to T4 codon usage.

MeSH Terms
Base Sequence Escherichia coli/genetics Nucleic Acid Conformation Phosphotransferases/metabolism Polynucleotide 5'-Hydroxyl-Kinase/metabolism Polynucleotide Ligases/metabolism RNA Ligase (ATP)/metabolism RNA Processing, Post-Transcriptional RNA, Bacterial/genetics RNA, Transfer, Amino Acyl/genetics Ribonucleases/metabolism T-Phages/enzymology,genetics
Chemicals
RNA, Bacterial RNA, Transfer, Amino Acyl Phosphotransferases Polynucleotide 5'-Hydroxyl-Kinase Ribonucleases anticodon nuclease Polynucleotide Ligases RNA Ligase (ATP)
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Amitsur M
Biochemistry Department, Tel Aviv University, Ramat Aviv, Israel.
Levitz R
Kaufmann G
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1987-08-00
Pages
2499-503
Language
English
Region
England
NLM ID
8208664
PMCID
PMC553660
Subset
IM
Grants
NIGMS NIH HHS · GM34124 · United States
Databases
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