Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DnaK chaperone system and the Sec machinery: completion of folding and Zn(II) ion acquisition occur in the bacterial periplasm.

Abstract

Metallo-beta-lactamases (MbetaLs) are zinc-dependent enzymes produced by many clinically relevant gram-negative pathogens that can hydrolyze most beta-lactam antibiotics. MbetaLs are synthesized in the bacterial cytoplasm as precursors and are secreted into the periplasm. Here, we report that the biogenesis process of the recently characterized MbetaL GOB… (More)
DOI: 10.1128/AAC.01637-08

Topics

Cite this paper

@article{MornBarrio2009SecretionOG, title={Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DnaK chaperone system and the Sec machinery: completion of folding and Zn(II) ion acquisition occur in the bacterial periplasm.}, author={Jorgelina Mor{\'a}n-Barrio and Adriana Sara Limansky and Alejandro Miguel Viale}, journal={Antimicrobial agents and chemotherapy}, year={2009}, volume={53 7}, pages={2908-17} }