Journal
FEMS MICROBIOLOGY LETTERS
Volume 212, Issue 1, Pages 7-13Publisher
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2002.tb11237.x
Keywords
serine/threonine protein kinase; ATP binding; activation loop; Ca2+; calmodulin binding; filamentous fungus
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A Ca2+/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-bin ding 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 Ca2+/calmodulin signaling in A. dactyloides. (C) 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
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