Document Detail


Proteome analysis of Acetobacter pasteurianus during acetic acid fermentation.
MedLine Citation:
PMID:  22155126     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Acetic acid bacteria (AAB) are Gram-negative, strictly aerobic microorganisms that show a unique resistance to ethanol (EtOH) and acetic acid (AcH). Members of the Acetobacter and Gluconacetobacter genera are capable of transforming EtOH into AcH via the alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) enzymes and are used for the industrial production of vinegar. Several mechanisms have been proposed to explain how AAB resist high concentrations of AcH, such as the assimilation of acetate through the tricarboxylic acid (TCA) cycle, the export of acetate by various transporters and modifications of the outer membrane. However, except for a few acetate-specific proteins, little is known about the global proteome responses to AcH. In this study, we used 2D-DIGE to compare the proteome of Acetobacter pasteurianus LMG 1262(T) when growing in glucose or ethanol and in the presence of acetic acid. Interesting protein spots were selected using the ANOVA p-value of 0.05 as threshold and 1.5-fold as the minimal level of differential expression, and a total of 53 proteins were successfully identified. Additionally, the size of AAB was reduced by approximately 30% in length as a consequence of the acidity. A modification in the membrane polysaccharides was also revealed by PATAg specific staining.
Authors:
Cristina Andrés-Barrao; Maged M Saad; Marie-Louise Chappuis; Mauro Boffa; Xavier Perret; Ruben Ortega Pérez; François Barja
Related Documents :
21590516 - Enantioselective recognition of tartaric acids with ethynylated carbazole-based chiral ...
22054676 - Amino acid composition of meat, fatty acid composition of fat and content of some chemi...
15790076 - Effect of age on the fatty acid composition of the bacillus subtilis po270 isolated fro...
1924096 - Partitioning of nutrients for growth and other metabolic functions: efficiency and prio...
11740946 - Interaction between the gln-arg 192 variants of the paraoxonase gene and oleic acid int...
2823886 - Kinetics of leukotriene a4 synthesis by 5-lipoxygenase from rat polymorphonuclear leuko...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-12-2
Journal Detail:
Title:  Journal of proteomics     Volume:  -     ISSN:  1876-7737     ISO Abbreviation:  -     Publication Date:  2011 Dec 
Date Detail:
Created Date:  2011-12-13     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101475056     Medline TA:  J Proteomics     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011. Published by Elsevier B.V.
Affiliation:
Department of Botany and Plant Biology, Microbiology Unit, University of Geneva, Chemin des Embrouchis 10, CH-1254 Jussy-Geneva, Switzerland.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Tissue-specific mutagenesis by N-butyl-N-(4-hydroxybutyl)nitrosamine as the basis for urothelial car...
Next Document:  Development of a Protein Standard Absolute Quantification (PSAQ™) assay for the quantification of ...