A calcium-dependent protein kinase with a regulatory domain similar to calmodulin

Journal Article · Fri May 17 04:00:00 EDT 1991 · Science (Washington, D.C.); (United States)

DOI:https://doi.org/10.1126/science.1852075· OSTI ID:5604982

Harper, J F; Sussman, M R; Schaller, G E ^[1]; Putnam-Evans, C ^[2]; Charbonneau, H ^[3]; Harmon, A C ^[4]

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1. Univ. of Wisconsin, Madison (United States)
2. Univ. of Georgia, Athens (United States)
3. Univ. of Washington, Seattle (United States)
4. Univ. of Florida, Gainesville (United States)

Calcium can function as a second messenger through stimulation of calcium-dependent protein kinases. A protein kinase that requires calcium but not calmodulin or phospholipids for activity has been purified from soybean. The kinase itself binds calcium with high affinity. A complementary DNA clone for this kinase has been identified; it encodes a protein with a predicted molecular mass of 57,175 daltons. This protein contains a catalytic domain similar to that of calmodulin-dependent kinases and a calmodulin-like region with four calcium binding domains (EF hands). The predicted structure of this kinase explains its direct regulation via calcium binding and establishes it as a prototype for a new family of calcium-regulated protein kinases.

• OSTI ID: 5604982
• Journal Information: Science (Washington, D.C.); (United States), Journal Name: Science (Washington, D.C.); (United States) Vol. 252:5008; ISSN SCIEA; ISSN 0036-8075
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AFFINITY
ALKALINE EARTH METALS
BIOCHEMICAL REACTION KINETICS
CALCIUM
CALMODULIN
CLONING
DNA HYBRIDIZATION
DNA-CLONING
ELEMENTS
ENZYME ACTIVITY
ENZYMES
FRACTIONATION
HYBRIDIZATION
KINETICS
METALS
MOLECULAR STRUCTURE
ORGANIC COMPOUNDS
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHOTRANSFERASES
PROTEINS
REACTION KINETICS
SEPARATION PROCESSES
TRANSFERASES