{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang CK"],"funding":["NIH, United States","NIGMS NIH HHS"],"pagination":["901-5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4036616"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["446(4)"],"pubmed_abstract":["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 for the secretion of enolase. Altering this helix by mutations showed that many mutated forms in this domain were not secreted, some of which were not stable as a soluble form in the cytoplasm. On the other hand, mutations on the flanking regions of the helix or the conserved basic residues showed no deleterious effect. Bacillus enolase with the proper hydrophobic helical domain was"],"journal":["Biochemical and biophysical research communications"],"pubmed_title":["An internal hydrophobic helical domain of Bacillus subtilis enolase is essential but not sufficient as a non-cleavable signal for its secretion."],"pmcid":["PMC4036616"],"funding_grant_id":["R01 GM034766","GM 34766"],"pubmed_authors":["Zhang XZ","Yang CK","Tai PC","Lu CD"],"additional_accession":[]},"is_claimable":false,"name":"An internal hydrophobic helical domain of Bacillus subtilis enolase is essential but not sufficient as a non-cleavable signal for its secretion.","description":"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 for the secretion of enolase. Altering this helix by mutations showed that many mutated forms in this domain were not secreted, some of which were not stable as a soluble form in the cytoplasm. On the other hand, mutations on the flanking regions of the helix or the conserved basic residues showed no deleterious effect. Bacillus enolase with the proper hydrophobic helical domain was","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Apr","modification":"2025-04-04T08:42:43.691Z","creation":"2019-03-27T01:28:59Z"},"accession":"S-EPMC4036616","cross_references":{"pubmed":["24642254"],"doi":["10.1016/j.bbrc.2014.03.032"]}}