Lateral interactions between protofilaments of the bacterial tubulin homolog FtsZ are essential for cell division.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 29889022.
- Also identified by DOI 10.7554/eLife.35578 and PMC identifier 6050046.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
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.
Medical subject headings
- Bacterial Proteins
- Cytoskeletal Proteins
- Escherichia coli
- Microfilament Proteins
- Tubulin