학술논문
Stress proteins in the cytoplasmic membrane fraction of Bacillus subtilis.
Document Type
Academic Journal
Author
Petráčková D; Department of Genetics and Microbiology, Faculty of Science, Charles University in Prague, 120 00 Prague, Czech Republic. d.petrackova@seznam.cz; Semberová L; Halada P; Svoboda P; Svobodová J
Source
Publisher: Springer Country of Publication: United States NLM ID: 0376757 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1874-9356 (Electronic) Linking ISSN: 00155632 NLM ISO Abbreviation: Folia Microbiol (Praha) Subsets: MEDLINE
Subject
Language
English
Abstract
Stress proteomes of the cytoplasmic membrane fraction of Bacillus subtilis trp (C2)-exposed to acid pH and ethanol were characterized. Although these stress factors impair the cell function in a specific manner, they share the ability to denature proteins. Therefore, specific and general stress proteins in the membranes were investigated. Both ethanol (3 %) and pH 5.0 increase the doubling time from 17 to 25 min. Isolated cytoplasmic membranes were subjected to an optimized 2D PAGE analysis which permitted the separation and analysis of ≈450 distinct protein spots. Two alternative methods of protein detection were compared, i.e. silver staining and (35)S-L-methionine pulse labeling; the stress induced proteins were identified by MALDI-TOF MS. After ethanol stress, five proteins were increased, viz. YdaP, Ctc, YfhM, YjcH and YwaC. Acid stress proteins were AcoB, YkwC, SodA, YjcH and YwaC. Proteins YjcH and YwaC were increased after ethanol as well as acid pH treatment.