In silico identification of functional divergence between the multiple groEL gene paralogs in Chlamydiae.

ABSTRACT:

Background

Heat-shock proteins are specialized molecules performing different and essential roles in the cell including protein degradation, folding and trafficking. GroEL is a 60 Kda heat-shock protein ubiquitous in bacteria and has been regarded as an important molecule implicated in chronic inflammatory processes caused by Chlamydiae infections. GroEL in Chlamydiae became duplicated at the origin of the Chlamydiae lineage presenting three distinct molecular chaperones, namely the original protein GroEL1 (Ct110), and its paralogous proteins GroEL2 (Ct604) and GroEL3 (Ct755). These chaperones present differential and independent expressions during the different stages of Chlamydiae infections and have been suggested to present differential physiological and regulatory roles.

Re

SUBMITTER: McNally D 

PROVIDER: S-EPMC1892554 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature