Abstract:
: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.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Tsai PJ,Tu J,Chen THdoi
10.1111/j.1574-6968.2002.tb11237.xkeywords:
subject
Has Abstractpub_date
2002-06-18 00:00:00pages
7-13issue
1eissn
0378-1097issn
1574-6968pii
S0378109702006481journal_volume
212pub_type
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