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Article

An internal hydrophobic helical domain of Bacillus subtilis enolase is essential but not sufficient as a non-cleavable signal for its secretion.

Biochemical and biophysical research communications - 18 Apr 2014

Yang Chun-Kai, Zhang Xiao-Zhou, Lu Chung-Dar, Tai Phang C

Abstract excerpt

Many cytoplasmic proteins without a cleavable signal peptide, including enolase, are secreted during the stationary phase in Bacillus subtilis but the molecular mechanism is not yet clear. We previously identified a highly conserved embedded membrane domain in an internal hydrophobic α-helix of enolase that plays an important role in its secretion. In this study, we examined the role of the helix in more detail...

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Identifiers

PMID: 24642254
DOI: 10.1016/j.bbrc.2014.03.032
PMCID: PMC4036616

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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