Processing of bacteriophage T4 tRNAs

Prágai, B.; Apirion, David

doi:10.1016/0022-2836(81)90410-1

Cited by 22 publications

(18 citation statements)

References 26 publications

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“…The composition of each oligonucleotide was determined by further digestion with RNase A (see Materials and Methods). The oligonucleotide numbers follow those given previously by Pragai and Apirion [7,8]. The open circles demonstrate the content of 10.1-S RNA and the hatched circles, the content of the 5' fragment that is removed by RNase 111 while cleaving 10.5-S RNA.…”

Section: Accumulation Of 105-s Rna In Rnc Strainsmentioning

confidence: 74%

“…1A) that was previously described [8]. Composition analysis of the T1 fingerprint of the fast-migrating RNA product has revealed that it is similar to X1 RNA, that has been identified in vivo [7,8].…”

Section: Accumulation Of 105-s Rna In Rnc Strainsmentioning

confidence: 95%

“…

Infection of RNase 111-(mc) Escherichia coli cells with bacteriophage T4427, a deletion mutant missing seven out of the ten genes in the tRNA transcription unit, results in the accumulation of a tRNA precursor (10.5s RNA) that contains the sequences of tRNAG'", tRNALeU and species 1 RNA [Pragai and Apirion (1981) J . Mol.

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mentioning

confidence: 99%

“…The RNase I11 cleavage is required for proper processing of the precursor. Particularly in the absence of RNase 111, tRNAG'", which is the first tRNA in the transcripts, is missing [6,7,9, 111. Therefore, it became rather important to determine accurately the RNase I11 processing site.…”

mentioning

confidence: 99%

“…By using a deletion mutant (427) of T4 that contains the first two genes (tRNAG'" and tRNALe") and the last gene (species 1 RNA), a new precursor RNA molecule has been identified, 10.5-S RNA [6] and its processing investigated [7-91. An RNase I11 cleavage site was suggested from in vivo and in vitro studies [7,101. The RNase I11 cleavage is required for proper processing of the precursor.…”

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confidence: 99%

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The ribonuclease-III-processing site near the 5′ end of an RNA precursor of bacteriophage T4 and its effect on termination

Gurevitz

Apirion

2008

European Journal of Biochemistry

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Infection of RNase III− (rnc) Escherichia coli cells with bacteriophage T4Δ27, a deletion mutant missing seven out of the ten genes in the tRNA transciption unit, results in the accumulation of tRNA precursor (10.5‐SRNA) that contains the sequence of tRNAGln, tRNALeu and species 1 RNA [Pragai and Apirion (1981) J. Mol. Biol. 153, 619–630]. In vitro studies, using partially purified RNase III or cell extracts and 10.5‐S RNA as substrate, have revealed a cleavage site at the 5′ side of the molecule. A computerized secondry structure suggests that the RNase III cleavage site can be placed in a small bulge which could be part of a duplex structure and is adjacent to A‐A‐G and its complementry sequence U‐U‐U in the same relative relationship found for most RNase III cleavage sites were the adjacent sequences are (A‐A‐G/U‐U‐C). Under normal processing conditions (presence of RNase III) the 3′ end of the processed intermediate precursors, 10.1‐S and p2Sp1 RNAs, is C‐U‐U‐(U1–2)‐UOH, which is determined by a stem and loop structure that could serve as a rho‐independent termination single site. However, in the absence of RNase III, the accumulated 10.5‐S precursor RNA does not terminate at the same site and its 3′ end is shifted a few nucleotides downstream. Thus, RNase III, besides playing a role in processing of 10.5‐S RNA, also affects the termination of that molecule, even though both sites, the RNase III cleavage site and the termination site, are about 390 nucleotides apart.

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Section: Accumulation Of 105-s Rna In Rnc Strainsmentioning

confidence: 74%

Section: Accumulation Of 105-s Rna In Rnc Strainsmentioning

confidence: 95%

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mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The ribonuclease-III-processing site near the 5′ end of an RNA precursor of bacteriophage T4 and its effect on termination

Gurevitz

Apirion

2008

European Journal of Biochemistry

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RNA processing in prokaryotic cells

Apirion

Miczák

1993

BioEssays

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RNA processing in Escherichia coli and some of its phages is reviewed here, with primary emphasis on rRNA and tRNA processing. Three enzymes, RNase III, RNase E and RNase P are responsible for most of the primary endonucleolytic RNA processing events. The first two are proteins, while RNase P is a ribozyme. These three enzymes have unique functions and in their absence, the cleavage events they catalyze are not performed. On the other hand a relatively large number of exonucleases participate in the trimming of the 3' ends of tRNA precursor molecules and they can substitute for each other. Primary processing is the first event that happens to the nascent RNA molecule, while in secondary RNA processing, the substrate is a product of a primary processing event. Although most RNA processing occurs in RNP particles, it seems that only in secondary RNA processing is the RNP particle required for the reaction. Bacteria and especially bacteriophages contain self-splicing introns which in cases were probably acquired from other species.

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