scholarly journals Identification and characterization of sporulation gene spoVS from Bacillus subtilis.

1995 ◽  
Vol 177 (19) ◽  
pp. 5628-5635 ◽  
Author(s):  
O Resnekov ◽  
A Driks ◽  
R Losick
Keyword(s):  
Bacillus Subtilis ◽  
Identification And Characterization

Isolation, identification and characterization of Bacillus subtilis ZJB-063, a versatile nitrile-converting bacterium

2008 ◽  
Vol 77 (5) ◽  
pp. 985-993 ◽  
Author(s):  
Yu-Guo Zheng ◽  
Jing Chen ◽  
Zhi-Qiang Liu ◽  
Ming-Huo Wu ◽  
Liang-Ying Xing ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Identification And Characterization

scholarly journals ClpXP Protease Regulates the Signal Peptide Cleavage of Secretory Preproteins in Bacillus subtilis with a Mechanism Distinct from That of the Ecs ABC Transporter

2002 ◽  
Vol 184 (4) ◽  
pp. 1010-1018 ◽  
Author(s):  
Tiina Pummi ◽  
Soile Leskelä ◽  
Eva Wahlström ◽  
Ulf Gerth ◽  
Harold Tjalsma ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Protein Secretion ◽  
Cytoplasmic Membrane ◽  
Signal Peptidase ◽  
Clp Protease ◽  
Peptide Cleavage ◽  
Secretion Regulation ◽  
Identification And Characterization ◽  
Binding Component

ABSTRACT Identification and characterization of a suppressor mutation, sup-15, which partially restored secretion in the protein secretion-deficient Bacillus subtilis ecsA26 mutant, led us to discover a novel function of Clp protease. Inactivation of ClpP improved the processing of the precursor of AmyQ α-amylase exposed on the outer surface of the cytoplasmic membrane. A similar improvement of AmyQ secretion was conferred by inactivation of the ClpX substrate-binding component of the ClpXP complex. In the absence of ClpXP, the transcription of the sipS, sipT, sipV, and lsp signal peptidase genes was elevated two- to fivefold, a likely cause of the improvement of the processing and secretion of AmyQ and complementation of ecs mutations. Specific overproduction of SipT enhanced the secretion. These findings extend the regulatory roles of ClpXP to protein secretion. ClpXP also influenced the processing of the lipoprotein PrsA. A concerted regulation of signal peptidase genes by a ClpXP-dependent activator is suggested. In contrast, Ecs did not affect transcription of the sip genes, pointing to a different mechanism of secretion regulation.

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