ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics Export

@article{citeulike:5076584, abstract = {10.1073/pnas.0904886106 FtsZ is the major cytoskeletal protein in bacteria and a tubulin homologue. It polymerizes and forms a ring where constriction occurs to divide the cell. We found that FtsZ is degraded by ClpXP, an ATP-dependent protease. In vitro, ClpXP degrades both FtsZ protomers and polymers; however, polymerized FtsZ is degraded more rapidly than the monomer. Deletion analysis shows that the N-terminal domain of ClpX is important for polymer recognition and that the FtsZ C terminus contains a ClpX recognition signal. In vivo, FtsZ is turned over slower in a deletion mutant compared with a WT strain. Overexpression of ClpXP results in increased FtsZ degradation and filamentation of cells. These results suggest that ClpXP may participate in cell division by modulating the equilibrium between free and polymeric FtsZ via degradation of FtsZ filaments and protomers.}, author = {Camberg, Jodi L. and Hoskins, Joel R. and Wickner, Sue}, citeulike-article-id = {5076584}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0904886106}, citeulike-linkout-1 = {http://www.pnas.org/content/106/26/10614.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/106/26/10614.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19541655}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19541655}, day = {30}, doi = {10.1073/pnas.0904886106}, journal = {Proceedings of the National Academy of Sciences}, keywords = {clpxp, coli, escherichia, ftsz}, month = {June}, number = {26}, pages = {10614--10619}, posted-at = {2009-07-06 17:01:01}, priority = {2}, title = {ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics}, url = {http://dx.doi.org/10.1073/pnas.0904886106}, volume = {106}, year = {2009} }

TY - JOUR ID - citeulike:5076584 L3 - citeulike-article-id:5076584 N2 - 10.1073/pnas.0904886106 FtsZ is the major cytoskeletal protein in bacteria and a tubulin homologue. It polymerizes and forms a ring where constriction occurs to divide the cell. We found that FtsZ is degraded by ClpXP, an ATP-dependent protease. In vitro, ClpXP degrades both FtsZ protomers and polymers; however, polymerized FtsZ is degraded more rapidly than the monomer. Deletion analysis shows that the N-terminal domain of ClpX is important for polymer recognition and that the FtsZ C terminus contains a ClpX recognition signal. In vivo, FtsZ is turned over slower in a deletion mutant compared with a WT strain. Overexpression of ClpXP results in increased FtsZ degradation and filamentation of cells. These results suggest that ClpXP may participate in cell division by modulating the equilibrium between free and polymeric FtsZ via degradation of FtsZ filaments and protomers. IS - 26 JF - Proceedings of the National Academy of Sciences EP - 10619 TI - ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics VL - 106 SP - 10614 KW - clpxp KW - coli KW - escherichia KW - ftsz AU - Camberg, Jodi AU - Hoskins, Joel AU - Wickner, Sue PY - 2009/06/30/ UR - http://dx.doi.org/10.1073/pnas.0904886106 ER -