Calcium, calmodulin-dependent protein phosphorylation in Neurospora crassa

6533b7d6fe1ef96bd1265d3b

RESEARCH PRODUCT

Calcium, calmodulin-dependent protein phosphorylation in Neurospora crassa

Ruben Ortega Pérez Gilbert Turian Dieter Marmé Diederik Van Tuinen

subject

[SDE] Environmental Sciences Calmodulin [SDV]Life Sciences [q-bio]Biophysics chemistry.chemical_element Calcium Biochemistry Neurospora Protein kinase Neurospora crassa 03 medical and health sciences Affinity chromatography Calmodulin Structural Biology Genetics [SDV.BV]Life Sciences [q-bio]/Vegetal Biology Protein phosphorylation [SDV.BV] Life Sciences [q-bio]/Vegetal Biology Protein kinase A Molecular Biology ComputingMilieux_MISCELLANEOUS 030304 developmental biology 0303 health sciences biology Neurospora crassa 030306 microbiology Cell Biology biology.organism_classification [SDV] Life Sciences [q-bio]chemistry Biochemistry [SDE]Environmental Sciences biology.protein Phosphorylation Calcium

description

Abstract A calcium, calmodulin-dependent protein kinase activity has been partially purified by calmodulin-Sepharose affinity chromatography from the soluble fraction of Neurospora crassa . The phosphorylated peptide has an apparent molecular mass on SDS-polyacrylamide gel of 47 kDa. The apparent half maximal phosphorylation is obtained after 1.5 min at 30° C in the presence of calcium and calmodulin. The apparent half maximal activation of the phosphorylation is obtained at 1 μM calcium, and 0.1 or 0.2 μM calmodulin from bovine brain or Neurospora , respectively. The 32 P incorporation is enhanced about 10-fold by calmodulin.

year	journal	country	edition	language
1984-10-29

https://hal.inrae.fr/hal-02726303

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