Calmodulin and calmodulin-binding proteins of Rhodosporidium toruloides, a basidiomycetous yeast
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چکیده
منابع مشابه
Calmodulin and calmodulin-binding proteins in brain.
filament preparations isolated from many different species. Incubation of crude and purified preparations of filaments with [f2P]ATP labels nearly all the filament proteins (Fig. l), the exception being the 65000-mol.wt. band of Loligo (Fig. la). Phosphorylation in vitro is mediated by a cyclic AMPand Ca2+-independent, and Mg2+-dependent, protein kinase. The enzyme is activated by Na+ and K+ an...
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Calmodulin is a small Ca2+-binding protein that acts to transduce second messenger signals into a wide array of cellular responses. Plant calmodulins share many structural and functional features with their homologs from animals and yeast, but the expression of multiple protein isoforms appears to be a distinctive feature of higher plants. Calmodulin acts by binding to short peptide sequences w...
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Calcium ion plays an important role in the hair cell's mechanoelectrical transduction process; in particular, Ca2+ controls adaptation to protracted mechanical stimuli. Because calmodulin is a ubiquitous intracellular receptor for Ca2+ and has been shown to accumulate at the tips of stereocilia, we determined its concentration and identified the proteins with which it interacts in the hair bund...
متن کاملCalmodulin-binding proteins and calmodulin-regulated enzymes in dog pancreas.
Calmodulin was isolated and purified to homogeneity from dog pancreas. Highly purified subcellular fractions were prepared from dog pancreas by zonal sucrose-density ultracentrifugation and assayed for their ability to bind 125I-calmodulin in vitro. Proteins contained in these fractions were also examined for binding of 125I-calmodulin after their separation by polyacrylamide-gel electrophoresi...
متن کاملCalmodulin and calmodulin-binding proteins in liver cell nuclei.
Three nuclear subfractions were prepared from isolated hepatocytes nuclei. The calmodulin content in whole nuclei was 79 ng/mg of protein. The soluble fraction obtained after digestion of the nuclei with DNase I and RNase A (S1 fraction) contained 252 ng of calmodulin/mg of protein. The pellet obtained after the digestion with nucleases was treated with 1.6 M NaCl, and the soluble fraction and ...
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ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1990
ISSN: 0022-1287
DOI: 10.1099/00221287-136-1-131