Cloning and functional characterization of a eucaryotic DNA photolyase gene from Neurospora crassa (original) (raw)

Journal Article

,

Search for other works by this author on:

,

1

Laboratory of Genetics, Department of Regulation Biology, Faculty of Science, Saitama University

Urawa 338, Japan

Search for other works by this author on:

,

Search for other works by this author on:

*To whom correspondence should be addressed at The Research Institute for Tuberculosis and Cancer, Tohoku University, Seiryomachi 4-1, Aobaku, Sendai 980, Japan

Search for other works by this author on:

Accepted:

05 September 1991

Published:

11 October 1991

• PDF
• Split View
• • Article contents
  • Figures & tables
  • Video
  • Audio
  • Supplementary Data
• Cite

Cite

Hirohiko Yajima, Hirokazu Inoue, Atsushi Oikawa, Akira Yasui, Cloning and functional characterization of a eucaryotic DNA photolyase gene from Neurospora crassa, Nucleic Acids Research, Volume 19, Issue 19, 11 October 1991, Pages 5359–5362, https://doi.org/10.1093/nar/19.19.5359
Close

Navbar Search Filter Mobile Enter search term Search

Abstract

We cloned a genomic fragment of a photolyase gene from Neurospora crassa by polymerase chain reaction using synthesized oligonucleotide primers designed from the most conserved amino acid sequences among photolyases of various organisms. Using the cloned fragment as a hybridization probe we isolated a genomic fragment and cDNA clones encoding the complete photolyase gene of this organism. The amino acid sequence of the photolyase deduced from the determined nucleotide sequence indicates a protein consisting of 615 amino acid residues (Mr 69,971), which is most similar to that of Saccharomyces cerevisiae. Like yeast photolyase it contains a protruding amino terminus which is missing in photolyases of bacterial origin. Comparison of amino acids sequences among six photolyases suggests that the Neurospora crassa photolyase is more similar to photolyases of pterin type than those of deazaflavin type.

This content is only available as a PDF.

© 1991 Oxford University Press

I agree to the terms and conditions. You must accept the terms and conditions.

Submit a comment

Name

Affiliations

Comment title

Comment

You have entered an invalid code

Thank you for submitting a comment on this article. Your comment will be reviewed and published at the journal's discretion. Please check for further notifications by email.

Citations

Views

Altmetric

Metrics

Total Views 76

25 Pageviews

51 PDF Downloads

Since 11/1/2016

Citations

40 Web of Science

×

Email alerts

Citing articles via

• Latest

• Most Read

• Most Cited

More from Oxford Academic