Open AccessPurification of a 47‐kDa calmodulin‐binding polypeptide as an actin‐binding protein from Neurospora crassa
Author(s) -
Capelli Nicolas,
Barja Francisco,
Tuinen Diederik,
Monnat Jean,
Turian Gilbert,
Ortega Perez Ruben
Publication year - 1997
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.1574-6968.1997.tb10244.x
Subject(s) - neurospora crassa , calmodulin , crassa , biology , binding protein , biochemistry , actin , affinity chromatography , actin binding protein , intracellular , microbiology and biotechnology , cytoskeleton , enzyme , cell , actin cytoskeleton , gene , mutant
We have enriched a 47‐kDa polypeptide (p47) from Neurospora crassa on the basis of its affinity to calmodulin. The p47 was purified to homogeneity by chromatography on a Mono S cation exchange column and evidence is presented that the polypeptide co‐sediments specifically with F‐actin. The intracellular distribution of p47 and actin was also examined using indirect double immunofluorescence staining of cells at different stages of development. Our results suggest that by altering the conformation binding site of actin to p47, calmodulin could play a regulatory role in the polarized hyphal growth of N. crassa .