Abstract
The optional Escherichia coli prr locus restricts phage T4 mutants lacking polynucleotide kinase or RNA ligase. Underlying this restriction is the specific manifestation of the T4-induced anticodon nuclease, an enzyme which triggers the cleavage-ligation of the host tRNALys. We report here the molecular cloning, nucleotide sequence and mutational analysis of prr-associated DNA. The results indicate that prr encodes a latent form of anticodon nuclease consisting of a core enzyme and cognate masking agents. They suggest that the T4-encoded factors of anticodon nuclease counteract the prr-encoded masking agents, thus activating the latent enzyme. The encoding of a tRNA cleavage-ligation pathway by two separate genetic systems which cohabitate E. coli may provide a clue to the evolution of RNA splicing mechanisms mediated by proteins.
MeSH Terms
Amino Acid Sequence
Base Sequence
Cloning, Molecular
DNA Mutational Analysis
Enzyme Activation/genetics
Escherichia coli/enzymology,genetics
Gene Expression Regulation, Bacterial/genetics
Molecular Sequence Data
RNA Splicing/genetics
RNA, Bacterial/metabolism
Ribonucleases/genetics,metabolism
T-Phages/genetics
Chemicals
RNA, Bacterial
Ribonucleases
anticodon nuclease
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Levitz R
Department of Biochemistry, Tel Aviv University, Ramat Aviv, Israel.
Chapman D
Amitsur M
Green R
Snyder L
Kaufmann G
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