Navigation auf zora.uzh.ch

Search ZORA

ZORA (Zurich Open Repository and Archive)

Migration von ZORA auf die Software DSpace

ZORA will change to a new software on 8th September 2025. Please note: deadline for new submissions is 21th July 2025!

Information & dates for training courses can be found here: Information on Software Migration.

DNA polymerase X from Deinococcus radiodurans possesses a structure-modulated 3'-->5' exonuclease activity involved in radioresistance.

Blasius, Melanie; Shevelev, Igor; Jolivet, Edmond; Sommer, Suzanne; Hübscher, Ulrich (2006). DNA polymerase X from Deinococcus radiodurans possesses a structure-modulated 3'-->5' exonuclease activity involved in radioresistance. Molecular Microbiology, 60(1):165-176.

Abstract

Recently a family X DNA polymerase (PolXDr) was identified in the radioresistant bacterium Deinococcus radiodurans. Knockout cells show a delay in double-strand break repair (DSBR) and an increased sensitivity to gamma-irradiation. Here we show that PolXDr possesses 3'-->5' exonuclease activity that stops cutting close to a loop. PolXDr consists of a DNA polymerase X domain (PolXc) and a Polymerase and Histidinol Phosphatase (PHP) domain. Deletion of the PHP domain abolishes only the structure-modulated but not the canonical 3'-->5' exonuclease activity. Thus, the exonuclease resides in the PolXc domain, but the structure-specificity requires additionally the PHP domain. Mutation of two conserved glycines in the PolXc domain leads to a specific loss of the structure-modulated exonuclease activity but not the exonuclease activity in general. The PHP domain itself does not show any activity. PolXDr is the first family X DNA polymerase that harbours an exonuclease activity. The wild-type protein, the glycine mutant and the two domains were expressed separately in DeltapolXDr cells. The wild-type protein could restore the radiation resistance, whereas intriguingly the mutant proteins showed a significant negative effect on survival of gamma-irradiated cells. Taken together our in vivo results suggest that both PolXDr domains play important roles in DSBR in D. radiodurans.

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:05 Vetsuisse Faculty > Veterinärwissenschaftliches Institut > Department of Molecular Mechanisms of Disease
07 Faculty of Science > Department of Molecular Mechanisms of Disease
Dewey Decimal Classification:570 Life sciences; biology
Scopus Subject Areas:Life Sciences > Microbiology
Life Sciences > Molecular Biology
Language:English
Date:1 April 2006
Deposited On:11 Feb 2008 12:18
Last Modified:01 Jul 2025 03:35
Publisher:Wiley-Blackwell
ISSN:0950-382X
OA Status:Closed
Publisher DOI:https://doi.org/10.1111/j.1365-2958.2006.05077.x
PubMed ID:16556228
Full text not available from this repository.

Metadata Export

Statistics

Citations

Dimensions.ai Metrics
28 citations in Web of Science®
30 citations in Scopus®
Google Scholar™

Altmetrics

Authors, Affiliations, Collaborations

Similar Publications