Self-assembling enzymes and the origins of the cytoskeleton
Author(s): Barry, Rachael M; Gitai, Zemer
DownloadTo refer to this page use:
http://arks.princeton.edu/ark:/88435/pr1td9n80n
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Barry, Rachael M | - |
dc.contributor.author | Gitai, Zemer | - |
dc.date.accessioned | 2024-02-19T16:31:37Z | - |
dc.date.available | 2024-02-19T16:31:37Z | - |
dc.date.issued | 2011-12 | en_US |
dc.identifier.issn | 1369-5274 | - |
dc.identifier.uri | http://arks.princeton.edu/ark:/88435/pr1td9n80n | - |
dc.description.abstract | 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 role. The behaviors of these enzymes suggest that some modern cytoskeletal proteins may have evolved from dual-role proteins with catalytic and structural functions. | en_US |
dc.language.iso | en_US | en_US |
dc.relation.ispartof | Current Opinion in Microbiology | en_US |
dc.rights | Author's manuscript | en_US |
dc.title | Self-assembling enzymes and the origins of the cytoskeleton | en_US |
dc.type | Journal Article | en_US |
dc.identifier.doi | doi:10.1016/j.mib.2011.09.015 | - |
pu.type.symplectic | http://www.symplectic.co.uk/publications/atom-terms/1.0/journal-article | en_US |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Self-assembling enzymes and the origins of the cytoskeleton.pdf | 839.3 kB | Adobe PDF | View/Download |
Items in OAR@Princeton are protected by copyright, with all rights reserved, unless otherwise indicated.