Biochemical evidence for the presence of an unconventional actin protein in a prokaryotic organism

被引：6

作者：

Labbe, JP ^{[1
]}

Harricane, MC ^{[1
]}

Boyer, M ^{[1
]}

Derancourt, J ^{[1
]}

Roustan, C ^{[1
]}

Benyamin, Y ^{[1
]}

机构：

[1] UNIV MONTPELLIER 1, EPHE,LAB RECH MOTIL CELLULAIRE,INSERM,U249,CNRS, UPR 8402, F-34033 MONTPELLIER, FRANCE

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1996年 / 114卷 / 03期

关键词：

prokaryote; actin; cyanobacteria; synechocystis; motility; cytoskeletal; evolution;

D O I：

10.1016/0305-0491(96)00034-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The ubiquity of actin, like the functional diversity of many associated proteins, raises a question concerning diversification of motility mechanisms and thus the emergence of an elementary functional system. Our aim was to investigate, in particular, mobiles prokaryotics cells as Synechocystis lacking cilia and flagella, search for actin essential properties and then locate the molecular behaviours. Here we report the presence and purification of a 56-kDa (apparent molecular weight) prokaryotic protein that polymerizes to form filaments, activates myosin Mg++-ATPase activity, inhibits DNase-1 activity and affords close antigenic homology to skeletal actin. This protein was found to be associated with thylakoid membranes and extracted in the presence of Triton X-100.

引用

页码：287 / 293

页数：7

共 45 条

[31] POLYAMINE-INDUCED ACTIN POLYMERIZATION [J].