SOS-inducible DNA repair proteins, RuvA and RuvB, of Escherichia coli: functional interactions between RuvA and RuvB for ATP hydrolysis and renaturation of the cruciform structure in supercoiled DNA - PubMed (original) (raw)

SOS-inducible DNA repair proteins, RuvA and RuvB, of Escherichia coli: functional interactions between RuvA and RuvB for ATP hydrolysis and renaturation of the cruciform structure in supercoiled DNA

T Shiba et al. Proc Natl Acad Sci U S A. 1991.

Abstract

The ruv operon is induced by treatments that damage DNA and is regulated by the LexA repressor. It encodes two proteins, RuvA and RuvB, that are involved in DNA repair, recombination in RecE and RecF pathways, and mutagenesis. RuvB protein was previously purified and has ATP-binding activity and weak ATPase activity. To study the biochemical properties of RuvA and its interaction with RuvB, we purified RuvA protein to near homogeneity from an over-producing strain. RuvA bound more efficiently to single-stranded DNA than to double-stranded DNA. RuvA bound to DNA greatly enhanced the ATPase activity of RuvB; the enhancing effect of various forms of DNA was in the order of supercoiled DNA greater than single-stranded DNA greater than linear double-stranded DNA. UV irradiation further enhanced the ATPase stimulatory effect of supercoiled DNA dose dependently. The RuvA-RuvB complex has an activity that renatures the cruciform structure in supercoiled DNA. From these experiments and previous work, we infer that the RuvA-RuvB complex may promote branch migration in recombination and may correct irregular structures in DNA, such as cruciforms and hairpins, to facilitate DNA repair using ATP as the energy source.

PubMed Disclaimer

Similar articles

• Properties of the Escherichia coli RuvA and RuvB proteins involved in DNA repair, recombination and mutagenesis.
  Shinagawa H, Shiba T, Iwasaki H, Makino K, Takahagi M, Nakata A. Shinagawa H, et al. Biochimie. 1991 Apr;73(4):505-7. doi: 10.1016/0300-9084(91)90120-p. Biochimie. 1991. PMID: 1911951 Review.
• Escherichia coli RuvA and RuvB proteins involved in recombination repair: physical properties and interactions with DNA.
  Shiba T, Iwasaki H, Nakata A, Shinagawa H. Shiba T, et al. Mol Gen Genet. 1993 Mar;237(3):395-9. doi: 10.1007/BF00279443. Mol Gen Genet. 1993. PMID: 8483454
• Novel properties of the Thermus thermophilus RuvB protein, which promotes branch migration of Holliday junctions.
  Yamada K, Fukuoh A, Iwasaki H, Shinagawa H. Yamada K, et al. Mol Gen Genet. 1999 Jul;261(6):1001-11. doi: 10.1007/s004380051049. Mol Gen Genet. 1999. PMID: 10485292
• Identification and characterization of Thermus thermophilus HB8 RuvA protein, the subunit of the RuvAB protein complex that promotes branch migration of Holliday junctions.
  Ohnishi T, Iwasaki H, Ishino Y, Kuramitsu S, Nakata A, Shinagawa H. Ohnishi T, et al. Genes Genet Syst. 2000 Oct;75(5):233-43. doi: 10.1266/ggs.75.233. Genes Genet Syst. 2000. PMID: 11245216
• Biological roles of the Escherichia coli RuvA, RuvB and RuvC proteins revealed.
  West SC, Connolly B. West SC, et al. Mol Microbiol. 1992 Oct;6(19):2755-9. doi: 10.1111/j.1365-2958.1992.tb01454.x. Mol Microbiol. 1992. PMID: 1435254 Review.

Cited by

• Enhancing Benzo[a]pyrene Degradation by Pantoea dispersa MSC14 through Biostimulation with Sodium Gluconate: Insights into Mechanisms and Molecular Regulation.
  Lai L, Li S, Zhang S, Liu M, Xia L, Ren Y, Cui T. Lai L, et al. Microorganisms. 2024 Mar 15;12(3):592. doi: 10.3390/microorganisms12030592. Microorganisms. 2024. PMID: 38543643 Free PMC article.
• Mechanism of AAA+ ATPase-mediated RuvAB-Holliday junction branch migration.
  Wald J, Fahrenkamp D, Goessweiner-Mohr N, Lugmayr W, Ciccarelli L, Vesper O, Marlovits TC. Wald J, et al. Nature. 2022 Sep;609(7927):630-639. doi: 10.1038/s41586-022-05121-1. Epub 2022 Aug 24. Nature. 2022. PMID: 36002576 Free PMC article.
• Comparison of transcriptional profiles of Treponema pallidum during experimental infection of rabbits and in vitro culture: Highly similar, yet different.
  De Lay BD, Cameron TA, De Lay NR, Norris SJ, Edmondson DG. De Lay BD, et al. PLoS Pathog. 2021 Sep 27;17(9):e1009949. doi: 10.1371/journal.ppat.1009949. eCollection 2021 Sep. PLoS Pathog. 2021. PMID: 34570834 Free PMC article.
• Thermal proteome profiling in bacteria: probing protein state in vivo.
  Mateus A, Bobonis J, Kurzawa N, Stein F, Helm D, Hevler J, Typas A, Savitski MM. Mateus A, et al. Mol Syst Biol. 2018 Jul 6;14(7):e8242. doi: 10.15252/msb.20188242. Mol Syst Biol. 2018. PMID: 29980614 Free PMC article.
• The helicase DinG responds to stress due to DNA double strand breaks.
  Frye SA, Beyene GT, Namouchi A, Gómez-Muñoz M, Homberset H, Kalayou S, Riaz T, Tønjum T, Balasingham SV. Frye SA, et al. PLoS One. 2017 Nov 9;12(11):e0187900. doi: 10.1371/journal.pone.0187900. eCollection 2017. PLoS One. 2017. PMID: 29121674 Free PMC article.

References

1. 1. Trends Genet. 1989 Nov;5(11):355-6 - PubMed
2. 1. Mol Gen Genet. 1989 Oct;219(1-2):328-31 - PubMed
3. 1. J Gen Microbiol. 1987 Sep;133(9):2531-8 - PubMed
4. 1. J Biol Chem. 1987 Sep 15;262(26):12752-8 - PubMed
5. 1. Nucleic Acids Res. 1986 Mar 25;14(6):2567-82 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Atypon
  • Europe PubMed Central
  • PubMed Central

• Molecular Biology Databases

  • BioCyc