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The FASEB Journal, Vol 2, 3010-3016, Copyright © 1988 by The Federation of American Societies for Experimental Biology

RESEARCH COMMUNICATIONS

Molecular cloning of a cDNA for the catalytic subunit of rabbit muscle phosphorylase phosphatase

G Bai, ZJ Zhang, J Amin, SA Deans-Zirattu and EY Lee
Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, Florida 33101.

A cDNA coding for the catalytic subunit of phosphorylase phosphatase (phosphatase C-I/phosphatase-1c) was cloned from a rabbit muscle cDNA library by screening with oligonucleotide probes. Ten clones were analyzed. The full cDNA sequence of 1395 base pairs contained an open reading frame of 990 base pairs flanked by 3' and 5' noncoding regions of 84 and 321 base pairs, respectively. The DNA sequence (and deduced amino acid sequence) of this cDNA is distinctly different from that of a clone of 1492 base pairs previously reported. Our cDNA is essentially identical to the 1492-base pair clone from residue 182 in the 3' direction, but it is completely different in the 5' direction. Consequently, the amino acid sequence deduced from our cDNA differs by 14 amino acids in the amino terminal from that previously reported and extends for an additional 19 amino acids. Probes to the divergent and common region of our cDNA clone hybridized to an mRNA of the same size by Northern blotting. Thus the cDNA we have isolated appears to code for an isoform of the catalytic subunit of phosphorylase phosphatase.


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Copyright © 1988 by The Federation of American Societies for Experimental Biology.