Bacteriophage T4 transfer RNA

Wilson, John H.; Kim, Jung Suh; Abelson, John

doi:10.1016/s0022-2836(72)80022-6

Cited by 108 publications

(13 citation statements)

References 15 publications

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“…In a preliminary attempt to characterize the template for these products, we examined whether their occurrence required any of the tRNA genes of T4 bacteriophage (19). Thus, employing a system from cells infected with T4 psu-b ASS [a deletion mutant lacking the entire tRNA region (14)], we obtained a pattern of 32P transfer products which was similar to that of the wild type and the complemented rli-system (Fig. 5).…”

mentioning

confidence: 81%

RNA ligase reaction products in plasmolyzed Escherichia coli cells infected by T4 bacteriophage.

David¹,

Vekstein²,

Kaufmann³

1979

Proc. Natl. Acad. Sci. U.S.A.

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Searching for a physiological role of T4 RNA ligase [polyribonucleotide synthetase (ATP); poly(ribonucleotide):poly(ribonucleotide) ligase (AMP-forming), EC 6.5.1.3] activity, we developed an acellular system of plasmolyzed Escherichia coli cells infected by T4 bacteriophage. Upon incubation of this system with 2p was transferred into a large number of polyribonucleotides, mostly up to 300-400 residues long. The bulk of 32P in the product polyribonucleotides was found in 5'-terminal phosphate groups, suggesting that they originated by a phosphorylation reaction catalyzed by the endogenous polynucleotide kinase (EC 2.7.1.78). Indeed, these products were not seen in an acellular system from uninfected cells, and their amount and complexity increased with the progress of infection. Analysis of the 32P-labeled olyribonucleotide products by gel electrophoresis, either before or after digestion with alkaline phosphatase (EC 3 The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. § 1734 solely to indicate this fact.

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mentioning

confidence: 81%

RNA ligase reaction products in plasmolyzed Escherichia coli cells infected by T4 bacteriophage.

David¹,

Vekstein²,

Kaufmann³

1979

Proc. Natl. Acad. Sci. U.S.A.

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“…The structural genes for these tRNAs seem to be clustered in a small region of the T4 genome, although it is not as yet clear whether these genes are transcribed as a single unit [3,4]. In the course of characterization of temperature sensitive mutants of E. coli defective in tRNA biosynthesis, we have demonstrated that none of the mature T4 tRNAs is synthesized in one of the mutants [S] .…”

Section: Introductionmentioning

confidence: 99%

Studies on T4‐tRNA biosynthesis: Accumulation of precursor tRNA molecules in a temperature sensitive mutant of Escherichia coli

1974

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“…These genes (psu-locus, ref. 21) are dispensable in many T4 host strains but there exist several strains in which one or more of the T4-coded tRNAs are needed (22,23 (Fig. 3) were not derived from leucine tRNA1 or from the CTr5x-specific cleavage products, because they occurred after infection with T4 mutants lacking either the extra arm or anticodon nuclease (our unpublished results).…”

Section: Discussionmentioning

confidence: 86%

“…The latter hosts (CT397 through CT511) as well as CT196 and CTr5x restrict T4 mutants lacking tRNA genes (psu-)j (refs. 21 GqVG in restricting rli and pnk-mutants (refs. 6.and 11 and-unpublished results).…”

mentioning

confidence: 99%

Bacteriophage T4-induced anticodon-loop nuclease detected in a host strain restrictive to RNA ligase mutants.

David¹,

Borasio²,

Kaufmann³

1982

Proc. Natl. Acad. Sci. U.S.A.

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The fate of host tRNAs during T4 bacteriophage infection was investigated with Escherichia coli CTr5x, the only known host strain that is restrictive to RNA ligase and polynucleotide kinase mutants. Three CTr5x tRNA species were cleaved during infection. One was leucine tRNA1, which was cleaved in the extra arm, as reported elsewhere for E. coli B infected with bacteriophage T2 or T4. The other two were specific to E. coli CTr5x and were not cleaved in various other hosts. One of the cleaved CTr5x-specific tRN-As had an anticodon sequence of the E. coli B "major" isoleucine tRNA but otherwise little sequence homology. Both CTrMx-specific tRNAs were cleaved by a distinct T4-induced endonuclease, other than that of leucine tRNA1, because the CTr5x-specific cleavages (i) were induced later in infection, (ii) persisted with a T4 mutant deficient in leucine tRNA1 endonuclease, and (iii) occurred in the anticodon loop. The specific manifestation of the anticodon-directed endonuclease activity in T4-infected E. coli CTr5x suggests roles for RNA ligase and polynucleotide kinase in processing of host tRNA species.RNA ligase from T4 bacteriophage [polyribonucleotide synthetase (ATP); poly(ribonucleotide):poly(ribonucleotide) ligase (AMPforming), EC 6.5.1.3; ref. 1] has been well characterized in vitro (2, 3), but its role in phage infection still needs to be determined (4-6). We have previously suggested that RNA ligase and additional T4 enzymes, such as polynucleotide kinase (EC 2.7.1.78; ref. 7) and a tRNA-specific endonuclease (8, 9), may constitute a pathway of host tRNA breakage and reunion (refs. 5 and 10 and Fig. 7). To examine this hypothesis we followed the fate of host tRNAs during T4 infection of Escherichia coli CTr5x (11). This host strain, and CT196, from which it was derived (11), are to date the only strains known to restrict polynucleotide kinase-3'-phosphatase (11)(12)(13) and RNA ligase (ref. 6 and unpublished results) mutants. It was expected, therefore, that E. coli CTr5x might feature a specific pattern oftRNA processing during T4 infection.We describe here a T4-induced endonuclease activity directed towards the anticodon loops of two E. coli CTr5x tRNAs. Its specific manifestation in E. coli CTr5x reinforces the idea about roles of RNA ligase and polynucleotide kinase in host tRNA metabolism. (14) supplemented by Ltryptophan at 20 Ag/ml, 0.1 mM CaCl2, and 0.4% glucose. METHODSWhen at 2-3 x 107 cells per ml, the culture was made up to 0.1 mCi/ml (1 Ci = 3.7 X 10"°becquerels) in [32P]Pi and growth continued to 2-4 x 10' cells per ml. The cells were centrifuged, resuspended in an equal volume of nonlabeled phosphate-rich SM9 medium (15), further grown for 15 min, and then infected with the T4 strain of choice at a multiplicity of infection of 6-12. The degree of infection was determined by plating aliquots before and during infection and counting bacterial colonies; it was found to be greater than 90% under these conditions. Culture aliquots were withdrawn either before or at progressive in...

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Bacteriophage T4 transfer RNA

Cited by 108 publications

References 15 publications

RNA ligase reaction products in plasmolyzed Escherichia coli cells infected by T4 bacteriophage.

RNA ligase reaction products in plasmolyzed Escherichia coli cells infected by T4 bacteriophage.

Studies on T4‐tRNA biosynthesis: Accumulation of precursor tRNA molecules in a temperature sensitive mutant of Escherichia coli

Bacteriophage T4-induced anticodon-loop nuclease detected in a host strain restrictive to RNA ligase mutants.

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