Secretion of nuclease across the outer membrane of Serratia marcescens and its energy requirements.
AUTOR(ES)
Suh, Y
RESUMO
Extracellular secretion of Serratia marcescens nuclease occurs as a two-step process via a periplasmic intermediate. Unlike other extracellular proteins secreted by gram-negative bacteria by the general secretory pathway, nuclease accumulates in the periplasm in its active form for an unusually long time before its export into the growth medium. The energy requirements for extracellular secretion of nuclease from the periplasm were investigated. Our results suggest that the second step of secretion across the outer membrane is dependent upon the external pH; acidic pH effectively but reversibly blocks extracellular secretion. However, electrochemical proton gradient, and possibly ATP hydrolysis, are not required for this step. We suggest that nuclease uses a novel mechanism for the second step of secretion in S. marcescens.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=178747Documentos Relacionados
- Two-step secretion of the Serratia marcescens extracellular nuclease.
- Differential secretion of isoforms of Serratia marcescens extracellular nuclease.
- Fermentation studies of the secretion of Serratia marcescens nuclease by Escherichia coli.
- Lipolytic activity copurified with the outer membrane of Serratia marcescens.
- Nuclease Overexpression Mutants of Serratia marcescens