Proteomic analyses of ethanol tolerance in Lactobacillus buchneri NRRL B‐30929. Issue 21 (22nd September 2014)

• Record Type: Journal Article
• Authors: Liu, Siqing
• Is Part Of: Proteomics. Volume 14:Issue 21/22(2014)
• Page Start: 2540
• Page End: 2544
• Publication Date: 2014-09-22
• Subjects: Proteins -- Separation -- Periodicals; Bioinformatics -- Periodicals; Proteomics -- Periodicals; Genomes -- Periodicals; Molecular genetics -- Periodicals; 572.605
• DOI: 10.1002/pmic.201300538
• Languages: English
• ISSNs: 1615-9853

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The <italic>Lactobacillus buchneri</italic> NRRL B‐30929 strain, isolated from a fuel ethanol (EtOH) production facility, exhibits high tolerance to environmental EtOH concentrations. This study aimed to identify proteins produced by B‐30929 in response to environmental EtOH. Cellular proteins expressed by B‐30929 growing in media with 10 versus 0% EtOH were compared by 2DE, followed by in‐gel digestion and MALDI‐MS analyses. Twenty EtOH responsive proteins were identified. These include a proline‐specific peptidase (<italic>Lbuc_1852</italic>); a membrane protein (<italic>Lbuc_0921</italic>), two general stress‐related proteins including a 10 kDa chaperonin (GroESL <italic>Lbuc_1359</italic>) and a 29 kDa member of the HK 97 family (<italic>Lbuc_1523</italic>); metabolic enzymes involving redox potential balances (<italic>Lbuc_2051</italic> and <italic>Lbuc_0522</italic>) and carbohydrate fermentation (<italic>Lbuc_1319</italic> and <italic>Lbuc_2157</italic>); nitrogen, amino acid, and fatty acid metabolism proteins (<italic>Lbuc_1994</italic>, <italic>Lbuc_0446</italic>, <italic>Lbuc_0858</italic>, <italic>Lbuc_0707</italic>, and <italic>Lbuc_0787</italic>). These changes suggested B‐30929 cells respond to EtOH by degradation of available proteins and fatty acids and increased production of specific enzymes and molecular chaperons. These results can be used to guide genetic modifications to increase EtOH tolerance in industrial biocatalysts. The data have been deposited to World‐2DPAGE (<ext-link ext-link-type="uri" xlink:href="http://world-2dpage.expasy.org/repository/0068/" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">http://world‐2dpage.expasy.org/repository/0068/</ext-link>; username liu, password 1h8d6Mg1).</p> </abstract>