A 3.4 kb PstI fragment containing the uvrC gene of Escherichia coli K-12 has been cloned into pBR322. Plasmids carrying this PstI fragment, in either orientation (pGY3233, pGY4211) relative to the cloning vehicle, complement uvrC mutants. A second plasmid (pGY3243) with a 21 kb HindIII fragment is shown to complement mutations in uvrA and ssb (single-strand binding protein). A composite plasmid (pGY4610) containing pBR322 and PstI fragments derived from pGY3233 (3.4 kb) and pGY3243 (11.05 kb) complements the uvrC, uvrA and ssb mutations.
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http://dx.doi.org/10.1016/0378-1119(80)90106-7 | DOI Listing |
Oncotarget
April 2018
School of Biomedical Sciences, Chung Shan Medical University, Taichung City, Taiwan.
Single-stranded DNA-binding proteins (SSBs) play crucial roles in DNA replication, repair, and recombination. Unlike , which contains only one type of SSB (EcSSB), some bacteria have two paralogous SSBs, namely, SsbA and SsbB. In this study, we found the third SSB-like protein in , SAAV2152, which was designated as SaSsbC.
View Article and Find Full Text PDFBiochim Biophys Acta Proteins Proteom
September 2017
Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai 400085, India; Homi Bhabha National Institute, Training School Complex, Anushakti Nagar, Mumbai 400094, India. Electronic address:
Deinococcus radiodurans is inherently resistant to both ionizing radiation and desiccation. Fifteen months of desiccation was found to be the LD dose for D. radiodurans.
View Article and Find Full Text PDFProteomics
December 2013
CNRS UMR 8621, Institut de Génétique et Microbiologie, Université Paris Sud, Orsay Cedex, France.
The nucleoids of radiation-resistant Deinococcus species show a high degree of compaction maintained after ionizing irradiation. We identified proteins recruited after irradiation in nucleoids of Deinococcus radiodurans and Deinococcus deserti by means of comparative proteomics. Proteins in nucleoid-enriched fractions from unirradiated and irradiated Deinococcus were identified and semiquantified by shotgun proteomics.
View Article and Find Full Text PDFRes Microbiol
April 2011
Department of Molecular Biology, Ruđer Bošković Institute, Bijenička 54, 10000 Zagreb, Croatia.
Homologous recombination is an essential process in double-strand break repair. The main requirement for recombination is formation of a RecA filament. Double-strand breaks can be processed into a RecA filament by the action of three enzymatic activities: helicase, 5'-3' exonuclease and RecA loading onto ssDNA.
View Article and Find Full Text PDFJ Bacteriol
August 2005
Centre de Recerca en Sanitat Animal (CReSA), 08193 Bellaterra, Spain.
The here-reported identification of the LexA-binding sequence of Bdellovibrio bacteriovorus, a bacterial predator belonging to the delta-Proteobacteria, has made possible a detailed study of its LexA regulatory network. Surprisingly, only the lexA gene and a multiple gene cassette including dinP and dnaE homologues are regulated by the LexA protein in this bacterium. In vivo expression analyses have confirmed that this gene cassette indeed forms a polycistronic unit that, like the lexA gene, is DNA damage inducible in B.
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