cDNA cloning of a calcineurin B homolog in Saccharomyces cerevisiae - PubMed (original) (raw)
Comparative Study
. 1991 Oct 31;180(2):1159-63.
doi: 10.1016/s0006-291x(05)81188-x.
Affiliations
- PMID: 1659397
- DOI: 10.1016/s0006-291x(05)81188-x
Comparative Study
cDNA cloning of a calcineurin B homolog in Saccharomyces cerevisiae
T Kuno et al. Biochem Biophys Res Commun. 1991.
Abstract
We have isolated a cDNA clone encoding a homolog of mammalian calcineurin B (the regulatory subunit of calmodulin-dependent protein phosphatase) by screening a cDNA expression library of Saccharomyces cerevisiae with antiserum against bovine calcineurin B. The yeast calcineurin B homolog (YCNB) is composed of 175 amino acids with a calculated molecular mass of 19,639 daltons and contains four putative Ca(2+)-binding domains. The amino-acid alignment of YCNB with human calcineurin B demonstrates 53% sequence identity and 82% homology. Southern blot analysis indicates that the gene for YCNB is a single-copy gene. Thus, yeast calmodulin-dependent protein phosphatase apparently has a heterodimeric structure similar to that of the enzyme in mammalians.
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