Show simple item record

dc.contributor.authorNiiranen, Laila
dc.contributor.authorLian, Kjersti
dc.contributor.authorJohnson, Kenneth A
dc.contributor.authorMoe, Elin
dc.date.accessioned2016-03-11T09:36:46Z
dc.date.available2016-03-11T09:36:46Z
dc.date.issued2015-02-27
dc.description.abstractBackground: Deinococcus radiodurans is an extremely radiation and desiccation resistant bacterium which can tolerate radiation doses up to 5,000 Grays without losing viability. We are studying the role of DNA repair and replication proteins for this unusual phenotype by a structural biology approach. The DNA polymerase III β subunit (β-clamp) acts as a sliding clamp on DNA, promoting the binding and processivity of many DNA-acting proteins, and here we report the crystal structure of D. radiodurans β-clamp (Drβ-clamp) at 2.0 Å resolution. <p>Results: The sequence verification process revealed that at the time of the study the gene encoding Drβ-clamp was wrongly annotated in the genome database, encoding a protein of 393 instead of 362 amino acids. The short protein was successfully expressed, purified and used for crystallisation purposes in complex with Cy5-labeled DNA. The structure, which was obtained from blue crystals, shows a typical ring-shaped bacterial β-clamp formed of two monomers, each with three domains of identical topology, but with no visible DNA in electron density. A visualisation of the electrostatic surface potential reveals a highly negatively charged outer surface while the inner surface and the dimer forming interface have a more even charge distribution. <p>Conclusions: The structure of Drβ-clamp was determined to 2.0 Å resolution and shows an evenly distributed electrostatic surface charge on the DNA interacting side. We hypothesise that this charge distribution may facilitate efficient movement on encircled DNA and help ensure efficient DNA metabolism in D. radiodurans upon exposure to high doses of ionizing irradiation or desiccation.en_US
dc.descriptionPublished version, also available at <a href=http://dx.doi.org/10.1186/s12900-015-0032-6>http://dx.doi.org/10.1186/s12900-015-0032-6</a>en_US
dc.identifier.citationBMC Structural Biology (2015) 15:5en_US
dc.identifier.cristinIDFRIDAID 1284184
dc.identifier.doi10.1186/s12900-015-0032-6
dc.identifier.issn1472-6807
dc.identifier.urihttps://hdl.handle.net/10037/8878
dc.identifier.urnURN:NBN:no-uit_munin_8461
dc.language.isoengen_US
dc.publisherBioMed Centralen_US
dc.rights.accessRightsopenAccess
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Basale biofag: 470::Genetikk og genomikk: 474en_US
dc.subjectVDP::Mathematics and natural science: 400::Basic biosciences: 470::Genetics and genomics: 474en_US
dc.subjectDNA polymerase III β subuniten_US
dc.subjectDeinococcus radioduransen_US
dc.subjectRadiation resistanceen_US
dc.titleCrystal structure of the DNA polymerase III β subunit (β-clamp) from the extremophile Deinococcus radioduransen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US


File(s) in this item

Thumbnail

This item appears in the following collection(s)

Show simple item record