Back to Search
Start Over
Characterization of CoPK02, a Ca2+/calmodulin-dependent protein kinase in mushroom Coprinopsis cinerea.
- Source :
-
Bioscience, Biotechnology & Biochemistry . Aug2018, Vol. 82 Issue 8, p1335-1343. 9p. - Publication Year :
- 2018
-
Abstract
- We surveyed genome sequences from the basidiomycetous mushroom Coprinopsis cinerea and isolated a cDNA homologous to CMKA, a calmodulin-dependent protein kinase (CaMK) in Aspergillus nidulans. We designated this sequence, encoding 580 amino acids with a molecular weight of 63,987, as CoPK02. CoPK02 possessed twelve subdomains specific to protein kinases and exhibited 43, 35, 40% identity with rat CaMKI, CaMKII, CaMKIV, respectively, and 40% identity with CoPK12, one of the CaMK orthologs in C. cinerea. CoPK02 showed significant autophosphorylation activity and phosphorylated exogenous proteins in the presence of Ca2+/CaM. By the CaM-overlay assay we confirmed that the C-terminal sequence (Trp346-Arg358) was the calmodulin-binding site, and that the binding of Ca2+/CaM to CoPK02 was reduced by the autophosphorylation of CoPK02. Since CoPK02 evolved in a different clade from CoPK12, and showed different gene expression compared to that of CoPK32, which is homologous to mitogen-activated protein kinase-activated protein kinase, CoPK02 and CoPK12 might cooperatively regulate Ca2+-signaling in C. cinerea. [ABSTRACT FROM AUTHOR]
- Subjects :
- *ASPERGILLUS nidulans
*PROTEIN kinases
Subjects
Details
- Language :
- English
- ISSN :
- 09168451
- Volume :
- 82
- Issue :
- 8
- Database :
- Academic Search Index
- Journal :
- Bioscience, Biotechnology & Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 130693855
- Full Text :
- https://doi.org/10.1080/09168451.2018.1462692