Regulation of the uvrC gene of Escherichia coli K12: localization and characterization of a damage-inducible promoter.

Sluis, C.A. van; Moolenaar, Geri F.; Backendorf, Claude

doi:10.1002/j.1460-2075.1983.tb01739.x

Cited by 45 publications

(26 citation statements)

References 38 publications

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“…Studies with poly(dA) -poly(dT) sequence segments in recombinant DNA molecules indicate that nucleosomes cannot form over an 80-bp poly(dA) * poly(dT) segment, and that poly(dA) * poly(dT) segments as small as 20 bp are disfavored during nucleosome formation (21,39 (52). The uvrA, uvrB, uvrC, and uvrD genes show about a fivefold induction similar to that observed for the RAD2 gene (17,20,50,51). However, the lacZ fusions of the RADI and RAD3 genes of S. cerevisiae do not show any evidence of increased P-galactosidase levels after DNA damaging treatments (30, 31, 44a).…”

Section: Resultsmentioning

confidence: 63%

Nucleotide sequence, transcript mapping, and regulation of the RAD2 gene of Saccharomyces cerevisiae

Madura¹,

Prakash²

1986

J Bacteriol

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We determined the nucleotide sequence, mapped the 5' and 3' mRNA termini, and examined the regulation of the RAD2 The RAD2 gene of Saccharomyces cerevisiae is one of 10 genes, RADI, RAD2, RAD3, RAI4, RAD7, RADIO, RAD14,-RAD16, RAD23, and MMS19, involved in excision repair of DNA containing pyrimidine dimers or cross-links (27,28,44,55). Mutants in the RADI, RAD2, RAD3, RAD4, RADIO, and MMSJ9 genes are highly defective in incision activity (27,44,55), while mutants in the other four genes show various degrees of incision defects (27,28,55). To study the structure, regulation, and function of these genes, we and others have cloned and characterized the RADI (15, 56), RAD2 (13, 33), RAD3 (14, 31, 32, 41), RAD7 (35), and RADIO (37, 42, 54) genes. We had previously located the and RADIO genes (15,37,42). In contrast, disruptions or deletions of the RAD3 gene are recessive lethal mutations (14,32,41). In this paper we report the complete nucleotide sequence of the RAD2 gene, map its 5' and 3' mRNA termini, and show that steady-state levels of RAIJ2 mRNA increase significantly after UV irradiation of yeast cells. MATERIALS AND METHODSYeast and bacterial strains. S. cerevisiae 7799-4B MATa his4-17 ura3-52 RAD+ was used for transcript analyses, and strain DBY746 MATa his3-Al leu2-3 leu2-112 trpl-289 ura3-52 RAD+ was used for RAD2-lacZ fusion analyses.

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Section: Resultsmentioning

confidence: 63%

Nucleotide sequence, transcript mapping, and regulation of the RAD2 gene of Saccharomyces cerevisiae

Madura¹,

Prakash²

1986

J Bacteriol

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“…A previous report indicates that ClpA is not a heat shock protein (17 (46,47). Thus, transcriptional regulation of the uvr genes varies, depending on the particular gene.…”

Section: Discussionmentioning

confidence: 98%

The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5

1990

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The genes that encode the subunits of the Clp protease of Escherichia coli, cipA and clpP, appear to be regulated differently from each other. The cipA gene does not seem to be under heat shock control (Y. S. Katayama, S. Gottesman, J. Pumphrey, S. Rudikoff, W. P. Clark, and M. R. Maurizi, J. Biol. Chem. 263:15226-15236, 1988). In contrast, the level of ClpP protein was increased in rpoH+ cells but not in null rpoH cells after an upshift in temperature from 17 to 43°C. The level of ClpP protein in a null dnaK strain was also elevated relative to the level of ClpP protein in an otherwise isogenic dnaK+ strain. In two-dimensional gels, the ClpP protein was located in the position of the previously unidentified heat shock protein F21.5. No protein spot corresponding to F21.5 was present in two-dimensional gels of a null clpP strain. The clpP gene, therefore, appears to be a heat shock gene, expressed in a &32-dependent manner and negatively regulated by DnaK; the product of clpP is the previously unidentified heat shock protein F21.5. When Escherichia coli cultures are shifted to an elevated growth temperature, a set of at least 17 heat shock proteins appears to be synthesized at an increased rate (26). The increased synthesis of these heat shock proteins depends upon the rpoH-encoded RNA polymerase cofactor au32, which specifically directs transcription from heat shock promoters (13). u32 is a positive effector of the heat shock response. DnaK protein, on the other hand, is a negative regulator of the E. coli heat shock response (41). In wild-type cells, the increased synthesis of heat shock proteins that occurs very soon after a temperature upshift gradually decreases to a new steady-state level by about 10 min after the upshift (48). dnaK mutant strains, however, do not turn off the heat shock response after a temperature upshift; dnaK mutants synthesize high levels of heat shock proteins at all temperatures (41).Neidhardt et al. (26) have located many heat shock proteins in autoradiographs of two-dimensional gels of extracts of heat-shocked E. coli cells. Through genetic and biochemical techniques, the identities of at least eight of the heat shock proteins found by autoradiography have been determined: GrpE (1), GroES (42), GroEL (24), DnaK (9), c70 (40), Lysyl-tRNA synthetase (14), DnaJ (4), and Lon (34).Lon, the well-characterized ATP-dependent protease of E. coli (8,12,23,49), is the only protease among the known heat shock proteins. A second ATP-dependent protease, referred to as Clp, has also been described (15,18). The Clp protease is composed of two components: an ATPase component, ClpA (16,17), and a proteolytic component, ClpP (16). Quantitation of immunoprecipitated ClpA protein from heat-shocked E. coli cells did not detect an increase in ClpA protein at elevated temperatures (17). Furthermore, ClpA synthesis remained unchanged at increased temperatures in a o2-defective strain, whereas the synthesis of heat shock proteins decreased (17). These observations led Katayama et al. (17) to conclude...

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“…There are conflicting reports as to the exact location of controlling region(s) and potential LexA protein binding sites that have been identified exhibit unusual features (Sharma et al . 1982, van Sluis et al . 1983, Sancar et al 1984, Foster and Strike 1985, Granger-Schnarr et al 1986) .…”

Section: Escherichia Colimentioning

confidence: 96%

The Molecular Genetics of the Incision Step in the DNA Excision Repair Process

Rubin

1988

International Journal of Radiation Biology

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This review describes the evolution of research into the genetic basis of how different organisms use the process of excision repair to recognize and remove lesions from their cellular DNA. One particular aspect of excision repair, DNA incision, and how it is controlled at the genetic level in bacteriophage, bacteria, S. cerevisae, D. melanogaster, rodent cells and humans is examined. In phage T4, DNA is incised by a DNA glycosylase-AP endonuclease that is coded for by the denV gene. In E. coli, the products of three genes, uvrA, uvrB and uvrC, are required to form the UVRABC excinuclease that cleaves DNA and releases a fragment 12-13 nucleotides long containing the site of damage. In S. cerevisiae, genes complementing five mutants of the RAD3 epistasis group, rad1, rad2, rad3, rad4 and rad10 have been cloned and analyzed. Rodent cells sensitive to a variety of mutagenic agents and deficient in excision repair are being used in molecular studies to identify and clone human repair genes (e.g. ERCC1) capable of complementing mammalian repair defects. Most studies of the human system, however, have been done with cells isolated from patients suffering from the repair defective, cancer-prone disorder, xeroderma pigmentosum, and these cells are now beginning to be characterized at the molecular level. Studies such as these that provide a greater understanding of the genetic basis of DNA repair should also offer new insights into other cellular processes, including genetic recombination, differentiation, mutagenesis, carcinogenesis and aging.

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Regulation of the uvrC gene of Escherichia coli K12: localization and characterization of a damage-inducible promoter.

Cited by 45 publications

References 38 publications

Nucleotide sequence, transcript mapping, and regulation of the RAD2 gene of Saccharomyces cerevisiae

Nucleotide sequence, transcript mapping, and regulation of the RAD2 gene of Saccharomyces cerevisiae

The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5

The Molecular Genetics of the Incision Step in the DNA Excision Repair Process

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