Evidence that ribosomal protein S10 participates in control of transcription termination.

Friedman, David I.; Schauer, Alan T.; Baumann, M. R.; Baron, L. S.; Adhya, Sankar

doi:10.1073/pnas.78.2.1115

Cited by 111 publications

(90 citation statements)

References 35 publications

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“…The same method as described above, measurement of accumulation of non-rRNA operon-encoded tRNAs relative to 5S RNA and tRNAGlU, was used to screen other nus mutations for effects on rRNA antitermination. No significant effect on the relative accumulation of these RNAs was detected in the nusAl (14), nusC60 (13), or nusE71 (13) mutant strains at 37TC or 42TC (data not shown), indicating that these mutants probably are not defective in rRNA transcription antitermination. However, a cold-sensitive nusA strain, K1914 (nusAcs; D. Friedman, personal communication), exhibited an increase in accumulation of nonrRNA operon-encoded tRNAs relative to 5S RNA and tRNAs encoded in rRNA operons when shifted to the nonpermissive temperature (data not shown), qualitatively similar to the increase observed in the nusB5 mutant, indicating that the nusA gene product may be involved in the antitermination mechanism used in transcription of rRNA operons.…”

Section: Methodsmentioning

confidence: 89%

See 1 more Smart Citation

Defective antitermination of rRNA transcription and derepression of rRNA and tRNA synthesis in the nusB5 mutant of Escherichia coli.

Sharrock¹,

Gourse²,

Nomura³

1985

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

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The nusB5 mutant of Escherichia coli was originally selected for reduced ability to support the antitermination of transcription that is mediated by the gene N product of bacteriophage X. By analyzing pulse-labeled RNA with an RNA-DNA ifiter hybridization technique, we have shown that, in the nusB5 mutant, the ratio of promoterproximal rRNA transcripts to promoter-distal transcripts is increased at least by a factor of 1.6; that is, in the absence of the functional nusB gene product, premature transcription termination takes place within rRNA operons. These results demonstrate that rRNA transcription in E. coli utilizes an antitermination mechanism that has at least one factor in common with the phage X system, the nusB gene product. We have also observed that the transcription initiation frequency at rRNA promoters is increased in the nusB5 strain and that this strain accumulates 30S and 50S ribosomal subunits at approximately the same rate as the parent. Thus, it appears thatE. coli compensates for premature termination of rRNA transcription by derepressing rRNA operon expression. The increase in rRNA promoter activity in the nusB5 mutant is accompanied by a parallel derepression of synthesis of tRNAs that are not encoded by rRNA operons. These results are consistent with a model for negative feedback regulation of rRNA and tRNA synthesis by products of rRNA operons.In Escherichia coli, transcription often terminates prematurely within polypeptide-encoding operons that contain nonsense mutations ("polar" mutations), presumably because the absence of translation exposes termination signals that are not normally active (1). Each of the seven rRNA operons of E. coli encodes =5000 bases of untranslated RNA that is processed to form the 16S, 23S, and 5S rRNAs as well as spacer and distal tRNAs (2, 3). It has been proposed that an antitermination mechanism functions during rRNA transcription to prevent premature termination within these operons (4, 5). In fact, it has been shown experimentally that termination sites within transposons and insertion elements (4,(6)(7)(8) Since the antitermination mechanism proposed for E. coli rRNA transcription may be similar to the phage X system (see ref. 5), we studied rRNA transcription in various nus mutants. The results presented in this paper show that premature transcription termination in fact takes place within rRNA operons in the nusB5 mutant. In addition, we analyzed the way in which regulation of rRNA and tRNA expression is altered in response to nusB5-induced premature termination of rRNA transcription. The results of these experiments are consistent with the feedback regulation model for rRNA and tRNA synthesis proposed (18, 19). (22). This probe covers the region from the fourth base downstream of the rrnB P2 start site to the 83rd nucleotide of mature 16S RNA (see Fig. 1). All other methods are described in the figure and table legends. MATERIALS AND METHODS RESULTS Premature Transcription Termination Within rRNAOperons Caused by the nusB5 Mutation. To stu...

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Section: Methodsmentioning

confidence: 89%

“…12), and ribosomal protein S10 (nusE; see ref. 13). Other mutations, nusA (14,15) and nusB (16), affect host proteins that, as yet, have been characterized only by their phenotypes relating to transcription antitermination (reviewed in ref.…”

mentioning

confidence: 99%

Defective antitermination of rRNA transcription and derepression of rRNA and tRNA synthesis in the nusB5 mutant of Escherichia coli.

Sharrock¹,

Gourse²,

Nomura³

1985

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

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“…Four Escherichia coli proteins function as cofactors in N-mediated antitermination: NusA, NusB, S10, and NusG (Friedman and Baron 1974;Keppel et al 1974;Friedman et al 1976Friedman et al , 1981Das and Wolska 1984;J. Li, R. Horwitz, S. McCracken, and J. Greenblatt, in prep.).…”

mentioning

confidence: 99%

The nut site of bacteriophage lambda is made of RNA and is bound by transcription antitermination factors on the surface of RNA polymerase.

Nodwell¹,

Greenblatt²

1991

Genes Dev.

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The boxA and boxB components of the k nut site are important for transcriptional antitermination by the phage N protein. We show here that boxA and boxB RNA in N-modified transcription complexes are inaccessible to ribonucleases and have altered sensitivity to dimethylsulfate. N and NusA suffice to weakly protect boxB, independently of boxA and other factors. However, efficient protection of the entire nut site from ribonucleases requires boxA and boxB, N, NusA, NusB, Sl0, and NusG. Mutations in RNA polymerase, which inhibit antitermination by N in vivo, disallow protection of the nut site during transcription in vitro; therefore, the surface of RNA polymerase must coordinate the formation of complexes containing the antitermination factors and nut site RNA.

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“…Antitermination by N involves the E. coli proteins NusA, NusB, NusG, and ribosomal protein S10 (Friedman and Baron 1974;Keppel et al 1974;Friedman et al 1976Friedman et al , 1981Das and Wolska 1984;Goda and Greenblatt 1985;Li et al 1992;. N-modified 3Corresponding author.…”

mentioning

confidence: 99%

Elongation factor NusG interacts with termination factor rho to regulate termination and antitermination of transcription.

Mason²,

Greenblatt³

1993

Genes Dev.

122

129

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NusG is a transcriptional elongation factor in Escherichia coli that aids transcriptional antitermination by the phage k N protein. By using NusG affinity chromatography, we found that NusG binds directly and selectively to termination factor p. NusG was shown previously to be needed for termination by p in vivo, and we show here that NusG increases the efficiency of termination by p at promoter-proximal sites in vitro. The rho026 mutation makes termination by p less dependent on NusG. It also makes antitermination by N at p-dependent terminators and the binding of p to NusG temperature sensitive. Therefore, the interaction of NusG with p is important both for p-dependent termination and for antitermination by N at p-dependent terminators.

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Evidence that ribosomal protein S10 participates in control of transcription termination.

Cited by 111 publications

References 35 publications

Defective antitermination of rRNA transcription and derepression of rRNA and tRNA synthesis in the nusB5 mutant of Escherichia coli.

Defective antitermination of rRNA transcription and derepression of rRNA and tRNA synthesis in the nusB5 mutant of Escherichia coli.

The nut site of bacteriophage lambda is made of RNA and is bound by transcription antitermination factors on the surface of RNA polymerase.

Elongation factor NusG interacts with termination factor rho to regulate termination and antitermination of transcription.

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