Purification of a 47-kDa calmodulin-binding polypeptide as an actin-binding protein from Neurospora crassa

Autor: François Barja, Nicolas Capelli, Gilbert Turian, Jean Monnat, Diederik Van Tuinen, Ruben Ortega Pérez
Přispěvatelé: UMR 0102 - Unité de Recherche Génétique et Ecophysiologie des Légumineuses, Génétique et Ecophysiologie des Légumineuses à Graines (UMRLEG) (UMR 102), Etablissement National d'Enseignement Supérieur Agronomique de Dijon (ENESAD)-Institut National de la Recherche Agronomique (INRA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Etablissement National d'Enseignement Supérieur Agronomique de Dijon (ENESAD)-Institut National de la Recherche Agronomique (INRA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, ProdInra, Migration
Jazyk: angličtina
Rok vydání: 2017
Předmět:
Hyphal growth
inorganic chemicals
congenital
hereditary
and neonatal diseases and abnormalities
Calmodulin
Cellular localization
Blotting
Western
01 natural sciences
Microbiology
Actin-binding protein
Neurospora crassa
03 medical and health sciences
hemic and lymphatic diseases
Genetics
Binding site
Fluorescent Antibody Technique
Indirect
[SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology
Molecular Biology
Actin
ComputingMilieux_MISCELLANEOUS
030304 developmental biology
0303 health sciences
Binding Sites
biology
Chemistry
010401 analytical chemistry
fungi
Crassa
biology.organism_classification
Chromatography
Agarose
Chromatography
Ion Exchange
Actins
3. Good health
0104 chemical sciences
ddc:580
[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology
Biochemistry
biology.protein
Electrophoresis
Polyacrylamide Gel
Peptides
Protein Binding
circulatory and respiratory physiology
Zdroj: FEMS Microbiology Letters
FEMS Microbiology Letters, Wiley-Blackwell, 1997, pp.215-220
FEMS Microbiology Letters, Vol. 147, No 2 (1997) pp. 215-220
ISSN: 0378-1097
1574-6968
Popis: 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.
Databáze: OpenAIRE
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