Welcome! Click here to login or here to register.
 |
|||||||||||||||||||
|
|||||||||||||||||||
 |
|||||||||||||||||||
"A cell division inhibitor SulA of Escherichia coli directly interacts with FtsZ through GTP hydrolysis." |
Higashitani A, Higashitani N, Horiuchi K |
Published April 6, 1995 in Biochem Biophys Res Commun volume 209 .
Pubmed ID: 7726836
Abstract:
| E. coli SulA is an SOS-inducible protein that inhibits cell division. FtsZ is a protein that plays a central role in bacterial cell division. Using purified SulA protein that was fused to the maltose binding protein, we demonstrate in vitro that SulA interacts with FtsZ to form a stable complex. The reaction requires GTP and Mg ion. GDP and GTP gamma S cannot substitute for GTP, which suggests that hydrolysis of GTP is required for the reaction. The complex is formed in a molar ratio of approximately one to one of the two proteins. It is likely that the complex formation represents the in vivo mechanism by which SulA inhibits cell division. |
This publication refers to following REPAIRtoire entries:
| Proteins |
Last modification of this entry: Oct. 11, 2010
Add your own comment!
There is no comment yet.
|
|
|
|