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

Capelli, Nicolas ; Barja, Francisco ; Van Tuinen, Diederik ; Monnat, Jean ; Turian, Gilbert ; Ortega Perez, Ruben

In: FEMS Microbiology Letters, 1997, vol. 147, no. 2, p. 215-220

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    Title
    • Purification of a 47-kDa calmodulin-binding polypeptide as an actin-binding protein from Neurospora crassa
    Author
    • Capelli, Nicolas. Laboratory of Biochemistry and Plant Physiology, 3 Place de l'Université, University of Geneva, CH-1211 Geneva 4, Switzerland
    • Barja, Francisco. Laboratory of General Microbiology, Sciences III, University of Geneva, CH-1211 Geneva 4, Switzerland
    • Van Tuinen, Diederik. Laboratory of Phytoparasitology, I.N.R.A.-SGAP, BV 1540, 21034 Dijon Cedex, France
    • Monnat, Jean. Laboratory of General Microbiology, Sciences III, University of Geneva, CH-1211 Geneva 4, Switzerland
    • Turian, Gilbert. Laboratory of General Microbiology, Sciences III, University of Geneva, CH-1211 Geneva 4, Switzerland
    • Ortega Perez, Ruben. Laboratory of General Microbiology, Sciences III, University of Geneva, CH-1211 Geneva 4, Switzerland
    Document Type
    • Postprint
    OAI-PMH Identifier
    • oai:doc.rero.ch:301116
    Summary
    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