Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-09

AUTHORS

Debabrata RayChaudhuri, James T. Park

ABSTRACT

ESCHERICHIA COLI divides by forming a septum across the middle of the cell. The biochemical mechanism underlying this process is unknown. Genetic evidence suggests that of all the fts (filamentation temperature sensitive) genes1,2 involved in E. coli cell division, ftsZ plays a central role at the earliest known step of septation3–5. Here we show that FtsZ protein binds GTP in vitro using unusual sequence elements6–8. In contrast, such binding to the product of the conditional-lethal ftsZ84 allele is impaired. Purified FtsZ displays a Mg2+-dependent GTPase activity which is markedly reduced in the FtsZ84 protein. FtsZ copurifies with near stoichiometric amounts of noncovalently-bound GDP, implying the presence of a GTPase cycle in vivo, similar to that known for signal-transducing GTP-binding proteins8,9. We also show that a small fraction of FtsZ exists as a distinct membrane-associated species that binds GTP. The membrane association of FtsZ and the known ability of GTPases to act as molecular switches8,9 implicate FtsZ in a GTP-activated signal transduction pathway that may regulate the start of septation in E. coli. More... »

PAGES

251-254

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/359251a0

DOI

http://dx.doi.org/10.1038/359251a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1007123869

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1528267


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