Kuno T, Tanaka H, Mukai H, Chang C D, Hiraga K, Miyakawa T, Tanaka C
Department of Pharmacology, Kobe University School of Medicine, Japan.
Biochem Biophys Res Commun. 1991 Oct 31;180(2):1159-63. doi: 10.1016/s0006-291x(05)81188-x.
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.
