The protein complex that synthesizes cell envelope material during separation is the Divisome. The Divisome is a multiprotein complex that is responsible for the coordinated assembly of the bacterial cell envelope. It is composed of a number of different proteins that are involved in the synthesis of the peptidoglycan layer, the outer membrane, and the cytoplasmic membrane. The Divisome is responsible for the biogenesis of the cell envelope and is essential for bacterial cell division.
The divider it is a protein complex at the bacteria who is responsible for cell divisionconstriction of the inner and outer membranes during division and peptidoglycan (PG) synthesis in place of division. The divisosome is a complex of membrane proteins with proteins on both sides of the cytoplasmic membrane. At the gram negative cells is located in the inner membrane. The didisome is almost ubiquitous in bacteria, although its composition can vary between species.
The elongate is a modified version of the didisome without the constriction of the membrane FtsZ-ring and its associated machines. The elongosome is present only in non-spherical bacteria and directs the lateral insertion of PG along the cell axis, thus allowing cylindrical growth (as opposed to spherical growth, as in coconuts).
Some of the first cell division genes from Escherichia coli were discovered by by François Jacob group in France in the 1960s. They were called foot genes, because mutants of these genes conferred a filumous ttemperature-ssensitive phenotype. At the non-permissive temperature (usually 42 °C), the fts mutant cells continue to elongate without dividing, forming filaments that can be up to 150
m long (as opposed to 2-3
m in wild-type cells). Three breakthroughs came with the discovery of the ftsZ gene in 1980 and the realization that the FtsZ protein was located in the plane of division of dividing cells, and finally the realization that the structure of FtsZ is remarkably similar to tubulin and that they likely share a common ancestor.
The precise composition of divisome and elongosome remains unknown, as they are highly dynamic protein complexes that recruit and release certain proteins during cell division. However, more than 20 proteins are known to be part of the divisome in E coli with a similar number of proteins in gram positive bacteria (such as Bacillus subtilis), although not all proteins are conserved in bacteria.
Several other fts genes, such as ftsA, ftsW, ftsQ, ftsI, ftsL, ftsK, ftsN, and ftsB, have all been found to be essential for cell division and associated with the divisomic complex and the FtsZ ring. The FtsA protein binds directly to FtsZ in the cytoplasm, and FtsB, FtsL, and FtsQ form an essential membrane-embedded subcomplex. FtsK and FtsW are larger proteins with multiple transmembrane domains. FtsI, also known as PBP3, is the didisome-specific transpeptidase required for division septum synthesis.
DNA replication and cell division
DNA replication in bacteria is closely linked to cell division. For example, blocking replication in B. subtilis results in elongated cells without adequate cell division. Bacterial DNA replication is initiated by the binding of DnaA (an ATPase) to the origin of replication (oriC) in the middle of the cell. FtsZ assembly appears to be linked to successful DNA replication with MatP and ZapB somehow coordinating the interactions between the division machinery and DNA replication during chromosomal segregation in E coli.
The precise process of divisome assembly is not well understood. It starts with the initial proteins FtsZ and its membrane anchor FtsA, and the ZipA, EzrA and Zaps proteins (ZapA, ZapB, ZapC, ZapD) that promote the formation of the FtsZ ring. While FtsA and especially FtsZ are highly conserved among bacteria, ZipA, which is a second membrane anchor for FtsZ in gamma-proteobacteria, EzrA and the Zap proteins are less conserved and are absent in some species. After the initial proteins, the FtsQLB subcomplex is added, followed by FtsI (transpeptidase), FtsW (transglycosylase) and FtsN. Both FtsI and FtsW are required for septal wall synthesis. FtsW is related to the putative elongation-specific transglycosylase RodA, another disomal protein. FtsN appears to have several functions: it stabilizes the divisome (at least when overexpressed), acts as a trigger for cytokinesis (through interactions with FtsI and FtsW), and activates FtsA-mediated recruitment of FtsQLB through direct binding of FtsA. However, while FtsA, FtsQLB, FtsI and FtsW are widely conserved, FtsN is limited to Gram-negative organisms (such as E. coli) and therefore it is not universally required.
The mitochondrial (eukaryotic) splitter
A protein complex that orchestrates the division of eukaryotic cells mitochondria has been called the “mitochondrial divisome”. It is conceptually and operationally similar to the bacterial cell division machinery, but consists (mainly) of different proteins. However, there seem to be some aspects conserved, for example in the red alga Cyanidioschyzon Merolaea mitochondrial FtsZ protein partially contracts the organelle, which allows the dynamic Dnm1 homologue to assemble with the mitochondrial division ring (MD) on the cytosolic face to induce fission. However, in many eukaryotes (including yeasts and animals), the didisome functions in the complete absence of the FtsZ contractile ring.
- Fission (biology) – Biological process
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