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Microbiology 155 (2009), 3005-3014; DOI  10.1099/mic.0.029223-0
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Microbiology 155 (2009), 3005-3014; DOI  10.1099/mic.0.029223-0
© 2009 Society for General Microbiology

DNA polymerase X from Deinococcus radiodurans implicated in bacterial tolerance to DNA damage is characterized as a short patch base excision repair polymerase

Nivedita P. Khairnar and Hari S. Misra

Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai-400 085, India

The Deinococcus radiodurans R1 genome encodes an X-family DNA repair polymerase homologous to eukaryotic DNA polymerase β. The recombinant deinococcal polymerase X (PolX) purified from transgenic Escherichia coli showed deoxynucleotidyltransferase activity. Unlike the Klenow fragment of E. coli, this enzyme showed short patch DNA synthesis activity on heteropolymeric DNA substrate. The recombinant enzyme showed 5'-deoxyribose phosphate (5'-dRP) lyase activity and base excision repair function in vitro, with the help of externally supplied glycosylase and AP endonuclease functions. A polX disruption mutant of D. radiodurans expressing 5'-dRP lyase and a truncated polymerase domain was comparatively less sensitive to {gamma}-radiation than a polX deletion mutant. Both mutants showed higher sensitivity to hydrogen peroxide. Excision repair mutants of E. coli expressing this polymerase showed functional complementation of UV sensitivity. These results suggest the involvement of deinococcal polymerase X in DNA-damage tolerance of D. radiodurans, possibly by contributing to DNA double-strand break repair and base excision repair.

Correspondence
Hari S. Misra
hsmisra{at}barc.gov.in

Abbreviations: AP, apurinic/apyrimidinic; BER, base excision repair; dRP, deoxyribose phosphate; MMC, mitomycin C; NER, nucleotide excision repair; PHP, polymerase and histidinol phosphatase; PolX, polymerase X; Polβ, polymerase β; T/P, template/primer; UDG, uracil DNA glycosylase

Two supplementary tables and four supplementary figures are available with the online version of this paper.






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