Cloning of human calcineurin A: Evidence for two isozymes and identification of a polyproline structural domain

Journal Article · Thu Nov 30 23:00:00 EST 1989 · Proceedings of the National Academy of Sciences of the United States of America; (USA)

DOI:https://doi.org/10.1073/pnas.86.23.9183· OSTI ID:6921340

Guerini, D; Klee, C B ^[1]

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1. National Institutes of Health, Bethesda, MD (USA)

Two types (I and II) of cDNAs encoding the large (A) subunit of calcineurin, a calmodulin-regulated protein phosphatase, were isolated from human basal ganglia and brainstem mRNA. The complete sequences of the two calcineurin clones are identical except for a 54-base-pair insert in the type I clone and different 3{prime} ends including part of the coding sequence for the C termini of the two proteins. These findings suggest that calcineurin A consists of at least two isozymes that may result from alternative splicing events. The two forms of the enzyme differ in the C terminus, which contains an inhibitory domain rapidly severed by limited proteolysis. With the exception of an 18-amino acid insert, the central parts of the molecules, which harbor the catalytic domains, are identical and show extended similarities with the entire catalytic subunits of protein phosphatases 1 and 2A, defining a distinct family of protein phosphatases. The 40-residue N-terminal fragment, specific for calcineurin, contains a sequence of 11 successive prolines that is also found to bovine brain calcineurin by peptide sequencing. A role in the calmodulin activation of calcineurin is proposed for this novel structural element.

• OSTI ID: 6921340
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 86:23; ISSN PNASA; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINES
AMINO ACID SEQUENCE
AMINO ACIDS
ANIMALS
AZOLES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BODY
BRAIN
CARBOXYLIC ACIDS
CENTRAL NERVOUS SYSTEM
CLONING
DAYS LIVING RADIOISOTOPES
DNA
DNA HYBRIDIZATION
DNA SEQUENCING
DNA-CLONING
ENZYMES
ESTERASES
HELA CELLS
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HYBRIDIZATION
HYDROLASES
ISOENZYMES
ISOTOPES
LIGHT NUCLEI
MAMMALS
MAN
MOLECULAR STRUCTURE
MUSCLES
NERVOUS SYSTEM
NUCLEI
NUCLEIC ACIDS
ODD-ODD NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANS
PHOSPHATASES
PHOSPHORUS 32
PHOSPHORUS ISOTOPES
PRIMATES
PROLINE
PYRROLES
PYRROLIDINES
RABBITS
RADIOISOTOPES
RECOMBINANT DNA
STRUCTURAL CHEMICAL ANALYSIS
VERTEBRATES