Structural highlights
Function
[FTSZ_MYCTU] Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells (By similarity). Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909]
Publication Abstract from PubMed
The prokaryotic tubulin homolog FtsZ polymerizes into protofilaments, which further assemble into higher-order structures at future division sites to form the Z-ring, a dynamic structure essential for bacterial cell division. The precise nature of interactions between FtsZ protofilaments that organize the Z-ring and their physiological significance remain enigmatic. In this study, we solved two crystallographic structures of a pair of FtsZ protofilaments,and demonstrated that they assemble in an antiparallel manner through the formation of two different inter-protofilament lateral interfaces. Our in vivo photocrosslinking studies confirmed that such lateral interactions occur in living cells, and disruption of the lateral interactions rendered cells unable to divide. The inherently weak lateral interactions enable FtsZ protofilaments to self-organize into a dynamic Z-ring. These results have fundamental implications for our understanding of bacterial cell division and for developing antibiotics that target this key process.
Lateral interactions between protofilaments of the bacterial tubulin homolog FtsZ are essential for cell division.,Guan F, Yu J, Yu J, Liu Y, Li Y, Feng XH, Huang KC, Chang Z, Ye S Elife. 2018 Jun 11;7. pii: 35578. doi: 10.7554/eLife.35578. PMID:29889022[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guan F, Yu J, Yu J, Liu Y, Li Y, Feng XH, Huang KC, Chang Z, Ye S. Lateral interactions between protofilaments of the bacterial tubulin homolog FtsZ are essential for cell division. Elife. 2018 Jun 11;7. pii: 35578. doi: 10.7554/eLife.35578. PMID:29889022 doi:http://dx.doi.org/10.7554/eLife.35578
