groE genes affect SOS repair in Escherichia coli

Liu, Shi-Kau; Tessman, Irwin

doi:10.1128/jb.172.10.6135-6138.1990

Cited by 24 publications

(15 citation statements)

References 26 publications

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“…Liu and Tessman have reported that groE mutations may have a greater effect on mutagenesis than they do on repair. The interactions between UmuC and GroEL and GroES, in addition to affecting the stability of UmuC, may alter its activity to promote mutagenic repair (17,18).…”

Section: Discussionmentioning

confidence: 99%

“…By analogy, the GroE proteins of E. coli may function in a similar fashion. Our previous work and the work of others have shown that the GroE proteins of E. coli are required for processes involved in DNA repair, i.e., UV mutagenesis (which is the specialized processing of UV-irradiated DNA that results in mutation introduction) (6) and Weigle reactivation (which is the repair of UV-irradiated bacteriophage) (17).…”

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confidence: 99%

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Coexpression of UmuD' with UmuC suppresses the UV mutagenesis deficiency of groE mutants

Donnelly

Walker

1992

J Bacteriol

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The GroE proteins of Escherichia coli are heat shock proteins which have also been shown to be molecular chaperone proteins. Our previous work has shown that the GroE proteins of E. coli are required for UV mutagenesis. This process requires the umuDC genes which are regulated by the SOS regulon. As part of the UV mutagenesis pathway, the product of the umuD gene, UmuD, is posttranslationally cleaved to yield the active form, UmuD'. In order to investigate what role the groE gene products play in UV mutagenesis, we measured UV mutagenesis in groE+ and groE strains which were expressing either the umuDC or umuD'C genes. We found that expression of umuD' instead of umuD will suppress the nonmutability conferred by the groE mutations. However, cleavage of UmuD to UmuD' is unaffected by mutations at the groE locus. Instead we found that the presence of UmuD' increased the stability of UmuC in groE strains. In addition, we obtained evidence which indicates that GroEL interacts directly with UmuC.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Coexpression of UmuD' with UmuC suppresses the UV mutagenesis deficiency of groE mutants

Donnelly

Walker

1992

J Bacteriol

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“…Originally discovered as a gene whose mutations, groE, can lead to the failure of morphogenesis of bacteriophage X and other phages (6,13,44,46,52), subsequent genetic analysis produced mutants in one of two components, groEL (mopA) or groES (mopB) (47), which are defective in either DNA and RNA synthesis (50), SOS-induced mutagenesis and Weigle (UV) reactivation of UV-irradiated phage (7,26,33,43), protein export (31), proteolysis (45), septation (12), coupling of replication between F factor and the chromosome (36), or ability to grow at some or all temperatures (11,20). Further experiments implicated alterations in GroE levels or configuration in indirect suppression of a variety of mutations in other genes such as ssb (32,41), rpoH (30), dna (10,23), and various biosynthetic genes (48).…”

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confidence: 99%

A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12

1994

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A series of COOH-terminal deletions of the chaperonin GroEL have been examined for effects in vivo at haploid copy number on the essential requirement of GroEL for cell growth. Strains with a deletion of up to 27 COOH-terminal amino acids were viable, but not viable strain could be isolated with a deletion of 28 or more codons. When substitutions were placed in the COOH-terminal amino acid Val-521 of the 27-amino-acid-deleted (delta 27) mutant, we found variable effect--Trp and Glu led to inviability, whereas Arg and Gly were viable but slow growing. The effects of the Arg substitution plus deletion (V521R delta) were examined in more detail. Whereas the delta 27 mutant with the wild-type residue Val-521 grew as well as a strain with wild-type GroEL, the V521R delta mutant strain (groEL202) exhibited a broad range of phenotypic defects. These include slow growth; filamentous morphology; a defect in plating lambda; absence of activity of expressed human ornithine transcarbamylase, as seen in other GroEL mutants; and several newly observed defects, such as absence of motility, sensitivity to UV light and mitomycin, a defect in one mode of specialized transduction, and inability to grow on rhamnose. Sucrose gradient analysis of extracts from the V521R delta cells showed a substantially reduced level of GroEL sedimenting at the normal 20S position of the assembled tetradecamer and a relatively large amount of more lightly sedimenting subunits. This indicates that the substitution-deletion mutation interferes with oligomeric assembly of GroEL into its functional form. This is discussed in light of the recently determined crystal structure of GroEL.

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“…Among these are the heat shock GroEL and GroES proteins, which are necessary for mutagenesis probably by stabilizing the UmuDC complex (8,22). Even though dinYis not involved in mutagenesis, it could be a member of the chaperonin family.…”

Section: Resultsmentioning

confidence: 99%

Characterization of dinY, a new Escherichia coli DNA repair gene whose products are damage inducible even in a lexA(Def) background

et al. 1993

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Bacteriophage Mu dX(Ap lac) was used to isolate a mutation in an Escherichia coli lexA(Def) strain representing a previously undescribed gene (dinY) which does not seem to be under the direct control of LexA. The insertion created a dinY::lacZ fusion in which beta-galactosidase expression required a DNA-damaging treatment (UV irradiation or mitomycin) and activable RecA protein. This strain showed a decreased Weigle reactivation of bacteriophage lambda. However, it was fully inducible for UV mutagenesis. Two-dimensional gel electrophoresis analysis identified two spots absent in the mutant which were both UV inducible only in the presence of activated RecA protein (RecA*). This finding suggests that the dinY::lacZ fusion lies in a gene either that is under the direct control of activated RecA or whose product undergoes RecA*-dependent posttranscriptional/posttranslational modification(s). The dinY gene may also control the expression of some other gene(s) and/or lie in an operon. The fusion was mapped at a position between 41 and 41.5 min on the E. coli chromosome, in the vicinity of the ruv operon.

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groE genes affect SOS repair in Escherichia coli

Cited by 24 publications

References 26 publications

Coexpression of UmuD' with UmuC suppresses the UV mutagenesis deficiency of groE mutants

Coexpression of UmuD' with UmuC suppresses the UV mutagenesis deficiency of groE mutants

A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12

Characterization of dinY, a new Escherichia coli DNA repair gene whose products are damage inducible even in a lexA(Def) background

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