Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (523K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (6)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Petersen, J. L.
Right arrow Articles by Small, G. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Petersen, J. L.
Right arrow Articles by Small, G. D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2001, Vol. 29, No. 21 4472-4481
© 2001 Oxford University Press

A gene required for the novel activation of a class II DNA photolyase in Chlamydomonas

Jason L. Petersen and Gary D. Small*

Cellular and Molecular Biology Research Group, University of South Dakota, 414 East Clark Street, Vermillion, SD 57069-2390, USA

DNA photolyases catalyze the blue light-dependent repair of UV light-induced damage in DNA. DNA photolyases are specific for either cyclobutane-type pyrimidine dimers or (6–4) photoproducts. PHR2 is a gene that in Chlamydomonas reinhardtii encodes a class II DNA photolyase which catalyzes the photorepair of cyclobutane-type pyrimidine dimers. Based on amino acid sequence analysis of PHR2, which indicates the presence of a chloroplast targeting sequence, PHR2 was predicted to encode the chloroplast photolyase of Chlamydomonas. Using a sensitive gene-specific in vivo repair assay, we found that overexpression of PHR2 in Chlamydomonas results in targeting of the protein to not only the chloroplast, but also to the nucleus. Overexpression of PHR2 photolyase in a photoreactivation-deficient mutant, phr1, results in a largely inactive product. The phr1 mutant was found to be deficient in both photorepair of a chloroplast gene, rbcL, and a nuclear gene, rDNA. These results suggest that PHR2 is the structural gene for the photolyase targeted to both the chloroplast and the nucleus, and that the PHR1 gene product is necessary for full activity of PHR2 protein. To our knowledge, the requirement for a second gene for full activity of a DNA photolyase is novel.

* To whom correspondence should be addressed. Tel: +1 605 677 5129; Fax: +1 605 677 6381; Email: gsmall{at}usd.edu


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant Physiol.Home page
M. Teranishi, K. Nakamura, H. Morioka, K. Yamamoto, and J. Hidema
The Native Cyclobutane Pyrimidine Dimer Photolyase of Rice Is Phosphorylated
Plant Physiology, April 1, 2008; 146(4): 1941 - 1951.
[Abstract] [Full Text] [PDF]

Home page
 Mol Biol EvolHome page
D. R. Denver, S. L. Swenson, and M. Lynch
An Evolutionary Analysis of the Helix-Hairpin-Helix Superfamily of DNA Repair Glycosylases
Mol. Biol. Evol., October 1, 2003; 20(10): 1603 - 1611.
[Abstract] [Full Text]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.