A proteomic analysis of secreted proteins from xylan-induced Bacillus sp. strain K-1.
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.
Chu
P W
PW
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Yap
M N
MN
Wu
C Y
CY
Huang
C M
CM
Pan
F M
FM
Tseng
M J
MJ
Chen
S T
ST
D001407:Bacillus / Q000187:drug effects* / Q000378:metabolism; D001426:Bacterial Proteins / Q000096:biosynthesis*; D003470:Culture Media; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D020543:Proteome / Q000096:biosynthesis*; D013997:Time Factors; D014990:Xylans / Q000494:pharmacology*
D001426:Bacterial Proteins; D003470:Culture Media; D020543:Proteome; D014990:Xylans