Repair of UV damage in Halobacterium salinarum. (1st June 2003)
- Record Type:
- Journal Article
- Title:
- Repair of UV damage in Halobacterium salinarum. (1st June 2003)
- Main Title:
- Repair of UV damage in Halobacterium salinarum
- Authors:
- McCready, S.
Marcello, L. - Abstract:
- Abstract : Halobacterium is one of the few known Archaea that tolerates high levels of sunlight in its natural environment. Photoreactivation is probably its most important strategy for surviving UV irradiation and we have shown that both of the major UV photoproducts, cyclobutane pyrimidine dimers (CPDs) and (6–4) photoproducts, can be very efficiently repaired by photoreactivation in this organism. There are two putative photolyase gene homologues in the published genome sequence of Halobacterium sp. NRC-1. We have made a mutant deleted in one of these, phr2, and confirmed that this gene codes for a CPD photolyase. (6–4) photoproducts are still photoreactivated in the mutant so we are currently establishing whether the other homologue, phr1, codes for a (6–4) photolyase. We have also demonstrated an excision repair capacity that operates in the absence of visible light but the nature of this pathway is not yet known. There is probably a bacteria-type excision-repair mechanism, since homologues of uvrA, uvrB, uvrC and uvrD have been identified in the Halobacterium genome. However, there are also homologues of eukaryotic nucleotide-excision-repair genes ( Saccharomy cescerevisiae RAD3, RAD25 and RAD2 ) so there may be multiple repair mechanisms for UV damage in Halobacterium .
- Is Part Of:
- Biochemical Society transactions. Volume 31:Number 3(2003)
- Journal:
- Biochemical Society transactions
- Issue:
- Volume 31:Number 3(2003)
- Issue Display:
- Volume 31, Issue 3 (2003)
- Year:
- 2003
- Volume:
- 31
- Issue:
- 3
- Issue Sort Value:
- 2003-0031-0003-0000
- Page Start:
- 694
- Page End:
- 698
- Publication Date:
- 2003-06-01
- Subjects:
- Archaea -- Halobacterium -- photolyase -- (6–4) photoproducts -- repair -- UV damage
Biochemistry -- Congresses
572 - Journal URLs:
- https://portlandpress.com/biochemsoctrans ↗
- DOI:
- 10.1042/bst0310694 ↗
- Languages:
- English
- ISSNs:
- 0300-5127
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library HMNTS - ELD Digital store
- Ingest File:
- 16105.xml