Isolation and characterization of a calmodulin-like protein from Halobacterium salinarium.
The first evidence for a calmodulin-like protein in an archaeon, Halobacterium salinarium, is reported here. The calmodulin-like protein, with a molecular mass of 24 kDa and an estimated pI of 4.8, stimulated cyclic nucleotide phosphodiesterase in a calcium-dependent manner. This stimulation could be suppressed by calmodulin inhibitors. The Ca(2+)-binding ability was verified by 45Ca autoradiography.
Membran- und Bewegungsphysiologie, Botanisches Institut I, Justus Liebig-Universität, Giessen, Germany.
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T
Rothärmel
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G
Wagner
D001426:Bacterial Proteins / Q000302:isolation & purification*; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D002147:Calmodulin / Q000302:isolation & purification*; D006217:Halobacterium / Q000737:chemistry*; D008970:Molecular Weight
D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D002147:Calmodulin; D002118:Calcium