Document Detail

FtsZ and the division of bacterial cell
MedLine Citation:
PMID:  17654828     Owner:  NLM     Status:  MEDLINE    
In this review we have tried to describe proteins and supermolecular structures which take part in the division of bacterial cell. The principal cell division protein of the most of prokaryotes is FtsZ, a homologue of eukaryotic tubulin. FtsZ just as tubulin is capable to bind and hydrolyze GTP. The division of bacterial cell begins with forming of so called divisome. The basis of such divisome is a contractile ring (Z ring); the ring encircles the cell about midcell. Z ring consists of a bundle of laterally bound protofilaments, which have been formed as a result of FtsZ polymerization. Z ring is rigidly bounded to cytozolic side of inner membrane with participation of FtsA, ZipA, FtsW and many other cell division proteins of divisome. The ring directs the process of cytokinesis transmitting power of constriction to membrane. Primary structures of members of the family of prokaryotic FtsZs differ from eukaryotic tubulines significantly except the region, where the site of GTP binding is placed. There is high degree of homology between structures of these proteins in the region. FtsZ is one of the most conservative proteins in prokaryotes, but ftsZ genes have not been found in completely sequenced genomes of several species of microorganisms. There are 2 species of mycoplasmas (Ureaplasma parvum and Mycoplasma mobile), Prostecobacter dejongeii, 10 species of chlamydia and 5 species of archaea among them. So these organisms divide without FtsZ. There are many open reading frames which encode proteins with unknown functions in genomes of U. parvum and M. mobile. The comparison of primary structures of these hypothetical proteins with structures of cell division proteins did not allow researchers to find similar proteins among them. We suppose that the process of cell division of these organisms should recruit proteins with function similar to FtsZ and having homologous with FtsZ or other cell division proteins spatial structures.
I E Vishniakov; S N Borkhsenius
Publication Detail:
Type:  English Abstract; Journal Article; Review    
Journal Detail:
Title:  Tsitologiia     Volume:  49     ISSN:  0041-3771     ISO Abbreviation:  Tsitologiia     Publication Date:  2007  
Date Detail:
Created Date:  2007-07-27     Completed Date:  2007-09-19     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0417363     Medline TA:  Tsitologiia     Country:  Russia (Federation)    
Other Details:
Languages:  rus     Pagination:  421-9     Citation Subset:  IM    
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MeSH Terms
Bacterial Physiological Phenomena*
Bacterial Proteins / chemistry,  physiology
Cell Division
Cytoskeletal Proteins / chemistry,  physiology
Guanosine Triphosphate / metabolism
Mycoplasma / physiology
Protein Binding
Reg. No./Substance:
0/Bacterial Proteins; 0/Cytoskeletal Proteins; 0/FtsZ protein, Bacteria; 86-01-1/Guanosine Triphosphate

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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