Secretion of nuclease across the outer membrane of Serratia marcescens and its energy requirements

Yousin Suh, Michael J. Benedik

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)677-683
Number of pages7
JournalJournal of Bacteriology
Volume179
Issue number3
StatePublished - 1997
Externally publishedYes

Fingerprint

Periplasm
Serratia marcescens
Serratia marcescens nuclease
Membranes
Secretory Pathway
Gram-Negative Bacteria
Protons
Hydrolysis
Adenosine Triphosphate
Growth
Proteins

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Secretion of nuclease across the outer membrane of Serratia marcescens and its energy requirements. / Suh, Yousin; Benedik, Michael J.

In: Journal of Bacteriology, Vol. 179, No. 3, 1997, p. 677-683.

Research output: Contribution to journalArticle

@article{88ba7ec70d9a43d183b97edde260c51e,
title = "Secretion of nuclease across the outer membrane of Serratia marcescens and its energy requirements",
abstract = "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.",
author = "Yousin Suh and Benedik, {Michael J.}",
year = "1997",
language = "English (US)",
volume = "179",
pages = "677--683",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "3",

}

TY - JOUR

T1 - Secretion of nuclease across the outer membrane of Serratia marcescens and its energy requirements

AU - Suh, Yousin

AU - Benedik, Michael J.

PY - 1997

Y1 - 1997

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0031028560&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031028560&partnerID=8YFLogxK

M3 - Article

VL - 179

SP - 677

EP - 683

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 3

ER -