Open AccessCloning of a Ca 2+ /calmodulin‐dependent protein kinase gene from the filamentous fungus Arthrobotrys dactyloides
Author(s) -
Tsai PuiJen,
Tu Jenn,
Chen TsungHsien
Publication year - 2002
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2002.tb11237.x
Subject(s) - calmodulin , biochemistry , biology , protein kinase a , camk , threonine , amino acid , protein kinase domain , kinase , serine , peptide sequence , microbiology and biotechnology , gene , phosphorylation , mutant , enzyme , autophosphorylation
A Ca 2+ /calmodulin‐dependent protein kinase (CaMK) gene was cloned and characterized from Arthrobotrys dactyloides , a nematode‐trapping fungus. The resulting 373‐amino‐acid protein, FCaMK, has significant homology to mammalian CaMKs. FCaMK contains a serine/threonine kinase domain followed by a calmodulin‐binding domain. The activation loop in FCaMK (amino acids 184–199) contains a phosphorylation site at threonine‐188, which could be the target of a kinase activator. Truncated FCaMK mutants revealed that amino acids 296–324 are essential for calmodulin binding. An oligopeptide designed from residues 297–324 formed a stable peptide–calmodulin complex of 1:1 stoichiometry. Southern blot analysis detected a single copy of the fcamk gene, suggesting that FCaMK plays an important role in Ca 2+ /calmodulin signaling in A. dactyloides .