Spasmin and a putative spasmin binding protein(s) isolated from solubilized spasmonemes

被引：13

作者：

Asai, H ^{[1
]}

Ninomiya, T ^{[1
]}

Kono, RI ^{[1
]}

Moriyama, Y ^{[1
]}

机构：

[1] Waseda Univ, Dept Phys, Tokyo 169, Japan

来源：

JOURNAL OF EUKARYOTIC MICROBIOLOGY | 1998年 / 45卷 / 01期

关键词：

Carchesium; calcium-binding protein; spasmin; spasmin-binding proteins; spasmoneme; Vorticella; Zoothamnium;

D O I：

10.1111/j.1550-7408.1998.tb05066.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The amino acid composition and hydrophobicity scale (hydropathy) of calcium-binding proteins contained in the contractile spasmoneme of Carchesium polypinum was compared with other calcium-binding proteins from eukaryotes. Spasmins which may bind at most 4 calcium ions simultaneously and initiate spasmoneme contraction cooperatively belong to a super family of proteins including centrin/caltractin and calmodulin. Based on chemical modification of tryptophan and methionine, these residues are involved in contraction but the spasmin proteins contain little or none of these amino acids. Based on this evidence, it is suggested that another, non-calcium binding protein(s) is involved in spasmoneme contraction.

引用

页码：33 / 39

页数：7

共 51 条

[1] STRUCTURES LINKING MYONEMES, ENDOPLASMIC-RETICULUM, AND SURFACE MEMBRANES IN CONTRACTILE CILIATE VORTICELLA [J].