PURIFICATION OF A 47-KDA CALMODULIN-BINDING POLYPEPTIDE AS AN ACTIN-BINDING PROTEIN FROM NEUROSPORA-CRASSA

Authors
CAPELLI N BARJA F VANTUINEN D MONNAT J TURIAN G PEREZ RO
Citation
N. Capelli et al., PURIFICATION OF A 47-KDA CALMODULIN-BINDING POLYPEPTIDE AS AN ACTIN-BINDING PROTEIN FROM NEUROSPORA-CRASSA, FEMS microbiology letters, 147(2), 1997, pp. 215-220
Citations number
21
Categorie Soggetti
Microbiology
Journal title
FEMS microbiology letters → ACNP
ISSN journal
03781097
Volume
147
Issue
2
Year of publication
1997
Pages
215 - 220
Database
ISI
SICI code
0378-1097(1997)147:2<215:POA4CP>2.0.ZU;2-G
Abstract
We have enriched a 47-kDa polypeptide (p47) from Neurospora crassa on the basis of its affinity to calmodulin. The p47 was purified to homog eneity by chromatography on a Mono S cation exchange column and eviden ce is presented that the polypeptide cc-sediments specifically with F- actin. The intracellular distribution of p47 and actin was also examin ed using indirect double immunofluorescence staining of cells at diffe rent stages of development. Our results suggest that by altering the c onformation binding site of actin to p47, calmodulin could play a regu latory role in the polarized hyphal growth of N. crassa.