Characterization of YmgF, a 72-residue inner membrane protein that associates with the Escherichia coli cell division machinery.

ABSTRACT: Formation of the Escherichia coli division septum is catalyzed by a number of essential proteins (named Fts) that assemble into a ring-like structure at the future division site. Many of these Fts proteins are intrinsic transmembrane proteins whose functions are largely unknown. In the present study, we attempted to identify a novel putative component(s) of the E. coli cell division machinery by searching for proteins that could interact with known Fts proteins. To do that, we used a bacterial two-hybrid system based on interaction-mediated reconstitution of a cyclic AMP (cAMP) signaling cascade to perform a library screening in order to find putative partners of E. coli cell division protein FtsL. Here we report the characterization of YmgF, a 72-residue integral membrane protein of unkno

SUBMITTER: Karimova G 

PROVIDER: S-EPMC2612424 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature