Nucleic Acids Research, 1988, Vol. 16, No. 10 4447-4463
© 1988
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Cloning and characterization of a photolyase gene from the cyanobacterium Anacystis nidulans
The Research Institute for Tuberculosis and Cancer, Tohoku University 4-1 Seiryomachi, 980 Sendai, Japan 1Department of Chemistry, Massachusetts Institute of Technology, Cambridge MA 02139, USA 2Department of Cell Biology and Genetics, Erasmus University PO Box 1738, 3000 Rotterdam, The Netherlands
*To whom requests for reprints should be sent
Received February 4, 1988. Revised April 8, 1988. Accepted April 8, 1988.
A 2 kb fragment was isolated from an Anacystis nidulans genomic DNA library by hybridization with synthetic oligonucleotide probes derived from the N-terminal amino acid sequence of Anacystis photolyase. This fragment contains a 1452 bp-long open reading frame encoding a polypeptide of 484 amino acids (Mr 54475). Antibodies raised against purified Anacystis photolyase reacted with extracts of cells harboring fused genes between lacz of Escherichia coli and this gene. A 40.7% similarity was found between the deduced amino acid sequences of Anacystis and E.coli photolyases, notwithstanding the difference in chromophore structure.
+Present address: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 45 Shattuck Street, Boston, MA 02115, USA
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