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Self-assembling enzymes and the origins of the cytoskeleton

Author(s): Barry, Rachael M; Gitai, Zemer

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dc.contributor.authorBarry, Rachael M-
dc.contributor.authorGitai, Zemer-
dc.date.accessioned2024-02-19T16:31:37Z-
dc.date.available2024-02-19T16:31:37Z-
dc.date.issued2011-12en_US
dc.identifier.issn1369-5274-
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr1td9n80n-
dc.description.abstractThe 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.isoen_USen_US
dc.relation.ispartofCurrent Opinion in Microbiologyen_US
dc.rightsAuthor's manuscripten_US
dc.titleSelf-assembling enzymes and the origins of the cytoskeletonen_US
dc.typeJournal Articleen_US
dc.identifier.doidoi:10.1016/j.mib.2011.09.015-
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

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