Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
3399240 | Current Opinion in Microbiology | 2011 | 8 Pages |
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.
► The list of proteins forming bacterial cytoskeletal structures is expanding. ► Some enzymes self-assemble into higher-order structures such as filaments. ► Assembly may regulate activity and be repurposed for structural roles. ► Dual-role filaments may have been the origin of the cytoskeleton.