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

被引：13
|
作者：
Capelli, N
Barja, F
vanTuinen, D
Monnat, J
Turian, G
Perez, RO
机构：
[1] UNIV GENEVA, LAB GEN MICROBIOL, CH-1211 GENEVA 4, SWITZERLAND
[2] UNIV GENEVA, LAB BIOCHEM & PLANT PHYSIOL, CH-1211 GENEVA 4, SWITZERLAND
[3] INRA, SGAP, LAB PHYTOPARASITOL, F-21034 DIJON, FRANCE
来源：
FEMS MICROBIOLOGY LETTERS | 1997年 / 147卷 / 02期
关键词：
Neurospora crassa; calmodulin; actin-binding protein; cellular localization;
D O I：
10.1016/S0378-1097(96)00527-7
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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 cc-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.
引用
收藏
页码：215 / 220
页数：6
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