Self-assembling enzymes and the origins of the cytoskeleton

被引:38
作者
Barry, Rachael M. [1 ]
Gitai, Zemer [1 ]
机构
[1] Princeton Univ, Dept Mol Biol, Princeton, NJ 08544 USA
基金
美国国家卫生研究院;
关键词
ACETYL-COA CARBOXYLASE; LIVER GLUTAMATE-DEHYDROGENASE; FATTY-ACID SYNTHESIS; CYTIDINE TRIPHOSPHATE SYNTHETASE; POLYMER-PROTOMER TRANSITION; ESCHERICHIA-COLI-CELLS; BACTERIAL CYTOSKELETON; ENDOPLASMIC-RETICULUM; TRANSMEMBRANE PROTEIN; TRANSCRIPTION FACTOR;
D O I
10.1016/j.mib.2011.09.015
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The bacterial cytoskeleton is composed of a complex and diverse group of proteins that self-assemble into linear filaments. These filaments support and organize cellular architecture and provide a dynamic network controlling transport and localization within the cell. Here, we review recent discoveries related to a newly appreciated class of self-assembling proteins that expand our view of the bacterial cytoskeleton and provide potential explanations for its evolutionary origins. Specifically, several types of metabolic enzymes can form structures similar to established cytoskeletal filaments and, in some cases, these structures have been repurposed for structural uses independent of their normal roles. The behaviors of these enzymes suggest that some modern cytoskeletal proteins may have evolved from dual-role proteins with catalytic and structural functions.
引用
收藏
页码:704 / 711
页数:8
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