The non-catalytic "cap domain" of a mycobacterial metallophosphoesterase regulates its expression and localization in the cell.

ABSTRACT: Despite highly conserved core catalytic domains, members of the metallophosphoesterase (MPE) superfamily perform diverse and crucial functions ranging from nucleotide and nucleic acid metabolism to phospholipid hydrolysis. Unique structural elements outside of the catalytic core called "cap domains" are thought to provide specialization to these enzymes; however, no directed study has been performed to substantiate this. The cap domain of Rv0805, an MPE from Mycobacterium tuberculosis, is located C-terminal to its catalytic domain and is dispensable for the catalytic activity of this enzyme in vitro. We show here that this C-terminal extension (CTE) mediates in vivo localization of the protein to the cell membrane and cell wall as well as modulates expression levels of Rv0805 in mycobacter

SUBMITTER: Matange N 

PROVIDER: S-EPMC4139253 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature