A temperature sensitive mutation of the β′‐subunit of DNA‐dependent RNA polymerase from <i>E. coli</i> T16

Panny, Susan R.; Heil, Alfred; Mazuś, B; Palm, Peter; Zillig, Wolfram; Mindlin, S. Z.; Ilyina, T. S.; Khesin, R. B.

doi:10.1016/0014-5793(74)80477-1

Cited by 43 publications

(7 citation statements)

References 23 publications

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“…The only inference as to the biochemical feature of 3' was a nonspecific DNA-binding capacity owing to the protein's positive charge (56). Temperature-sensitive lethal rpoC mutations have been isolated and prove that the ,B' subunit is essential for cell growth (43). Some of the P' mutations cause defects in the assembly of RNA polymerase (49).…”

Section: Discussionmentioning

confidence: 99%

Genetic interaction between the beta' subunit of RNA polymerase and the arginine-rich domain of Escherichia coli nusA protein

1991

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The nusAl) mutation causes reduced transcription termination and temperature-sensitive growth of Escherichia coil. Suppressor mutations that restored growth of nusAll mutant cells were isolated and named sna mutations. The intergenic suppressor mutation sna-10 was located in the rpoC gene at 90 min, which encodes the (3' subunit of RNA polymerase. sna-10 complemented the defect in tRl termination caused by nusAl) and by itself stimulated termination of transcription at the X tRl terminator. sna-10 is specific to the nusAl) allele and unable to suppress cold-sensitive growth of the nusAlO mutant. nusA10 carried two base substitutions at positions 311 and 634, causing two amino acid changes from the wild-type sequence. During these studies, we found three -1 frameshift errors in the wild-type nusA sequence; the correct sequence was confirmed by the peptide sequence and gene fusion analyses. The revised sequence revealed that nusAl and nusAl) are located in an arginine-rich peptide region and substitute arginine and aspartate for leucine 183 and glycine 181, respectively. The intragenic suppressor study indicated that the nusAl) mutation can be suppressed by cha ng the mutated aspartate 181 to alanine or changing aspartate 84 to tyrosine.

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Section: Discussionmentioning

confidence: 99%

Genetic interaction between the beta' subunit of RNA polymerase and the arginine-rich domain of Escherichia coli nusA protein

1991

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“…It is now evident that the similarity between vaccinia and cellular RNA polymerases extends to the molecular structure of at least one subunit. The amino acid sequence of may participate in DNA unwinding (27). In addition, a mutation in the largest subunit of Drosophila RNA polymerase II confers a reduced rate of RNA chain elongation in vitro (29).…”

Section: Discussionmentioning

confidence: 99%

Homology between RNA polymerases of poxviruses, prokaryotes, and eukaryotes: nucleotide sequence and transcriptional analysis of vaccinia virus genes encoding 147-kDa and 22-kDa subunits.

Broyles¹,

Moss²

1986

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

148

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We have determined the nucleotide sequence of a region of the vaccinia virus genome encoding RNA polymerase subunits of 22 and 147 kDa and have mapped the 5' and 3' ends of the two mRNAs. The predicted amino acid sequence of the vaccinia 147-kDa subunit shows extensive homology with the largest subunit of Escherichia coli RNA polymerase, yeast RNA polymerases II and m, and Drosophila RNA polymerase H. The regions of homology between the five RNA polymerases are subdivided into five separate domains that span most of the length of each. A sixth domain shared by the vaccinia and the eukaryotic polymerases is absent from the E. coli sequence. In all specified regions, the vaccinia large subunit has greater homology with eukaryotic RNA polymerases II and III than with the E. coli polymerase. Vaccinia virus and eukaryotic RNA polymerases may therefore have evolved from a common ancestral gene after the latter diverged from prokaryotes.The presence of a transcription and RNA-modification system within the core of vaccinia virus and other poxviruses contributes to their remarkable ability to replicate in the cytoplasm of animal cells (1). Because of its large size and multisubunit composition (2-4), the vaccinia virus RNA polymerase more closely resembles RNA polymerases of eukaryotic and prokaryotic organisms than those of viruses such as T7 (5). Nevertheless, the vaccinia virus RNA polymerase can be distinguished from that of its host with regard to the precise size of the subunits (2-4), a-amanitin insensitivity (3,4), and specificity for vaccinia virus promoters (6, 7). That soluble vaccinia virus extracts can initiate (8,9) and terminate (G. Rohrmann, L. Yuen, and B.M., unpublished data) transcription suggests that this system may have significant value as a research tool. Determination of the nature of the RNA polymerase is central both for our understanding of the biology and evolution of this extensive virus family and for evaluating its significance as an experimental model. We report here the nucleotide sequences of two vaccinia virus genes encoding RNA polymerase subunits and a computer analysis that reveals extensive similarities between the amino acid sequences of the large RNA polymerase subunits of vaccinia virus, Escherichia coli, yeast, and Drosophila.

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“…These combined resultst allowved us to assign group I) to the cistron encoding the (3 subunit of RNA polyrmerase, and group E to a cistron corresj)on(ling to another gene in the same operon. Group E mutations also failed to complement TsX, a teml)erature-sensitive RNA l)0ymerase mutation isolated by Khesin et al (8) which is known to be a is'mutation as shown by the in vitro reconstitution of the RNA polymerase from purified subunits (9). We, therefore, have assigned complemnentation group E to the structural gene for Olt.…”

Section: Itselfmentioning

confidence: 99%

Temperature-sensitive RNA polymerase mutants with altered subunit synthesis and degradation.

Kirschbaum¹,

Claeys²,

Nasi³

et al. 1975

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

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A temperature sensitive mutation of the β′‐subunit of DNA‐dependent RNA polymerase from E. coli T16

Cited by 43 publications

References 23 publications

Genetic interaction between the beta' subunit of RNA polymerase and the arginine-rich domain of Escherichia coli nusA protein

Genetic interaction between the beta' subunit of RNA polymerase and the arginine-rich domain of Escherichia coli nusA protein

Homology between RNA polymerases of poxviruses, prokaryotes, and eukaryotes: nucleotide sequence and transcriptional analysis of vaccinia virus genes encoding 147-kDa and 22-kDa subunits.

Temperature-sensitive RNA polymerase mutants with altered subunit synthesis and degradation.

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