A proteomic analysis of secreted proteins from xylan-induced Bacillus sp. strain K-1

• Published in: Electrophoresis Vol. 21; no. 9; pp. 1740 - 1745
• Main Authors: Chu, Pei-Wen, Yap, Mee-Ngan, Wu, Chi-Yue, Huang, Chun-Ming, Pan, Fu-Ming, Tseng, Min-Jen, Chen, Shui-Tein
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 01-05-2000
• Subjects: Bacillus - drug effects; Bacillus - metabolism; Bacillus sp; Bacterial Proteins - biosynthesis; Culture Media; Electrophoresis, Gel, Two-Dimensional - methods; Proteome - biosynthesis; Proteomics; Time Factors; Two-dimensional polyacrylamide gel electrophoresis; Xylan; Xylans - pharmacology
• ISSN: 0173-0835; 1522-2683
• DOI: 10.1002/(SICI)1522-2683(20000501)21:9<1740::AID-ELPS1740>3.0.CO;2-N

The expression level of extracellular proteins in an alkaliphilic bacterium, Bacillus sp. strain K‐1, grown in a xylan‐containing medium, is significantly increased when compared with that grown in the nonxylan culture medium. A proteomic approach has been efficiently applied to separate and characterize these differentially expressed secretory proteins. Eight prominent protein spots were identified and subjected to N‐terminal amino acid sequencing. The results show that three spots share considerable similarity with the xylanolytic enzymes and that two spots share considerable similarity with the GltC regulatory protein and 3‐dehydroquinate dehydratase, respectively. In addition, the three other proteins show little similarity with the known proteins in the database. In conclusion, our results demonstrate that the proteomic approach is a highly efficient method to rapidly study the differential expression of the secreted proteins by Bacillus sp. strain K‐1 grown under xylan‐induced condition.