Profile of native cellulosomal proteins of Clostridium cellulovorans adapted to various carbon sources

Abstract

We performed a focused proteome analysis of cellulosomal proteins predicted by a genome analysis of Clostridium cellulovorans [Tamaru, Y., et al.. 2010. J. Bacteriol. 192:901-902]. Our system employed a long monolithic column (300 cm), which provides better performance and higher resolution than conventional systems. Twenty-three cellulosomal proteins were, without purification, identified by direct analysis of the culture medium. Proteome analysis of the C. cellulovorans cellulosome after culture in various carbon sources demonstrated the production of carbon source-adapted cellulosome components.

Figure 1

Base peak chromatogram of a proteome sample extracted fromC. cellulovorans(A) monolithic column (300 cm), (B) conventional packed column (15 cm). A proteome sample prepared from C. cellulovorans was injected onto the column, and a (A) 600 or (B) 60 min gradient was applied with a flow rate of 500 nL/min.

Figure 2

Classification of produced cellulosomal enzymes ofC. cellulovoranscultivated with the various carbon sources, based on Table1.^a The number in the panel indicates identified enzymes cultivated with each carbon source. ^b The number indicates common enzymes identified in indicated carbon source. ^c The number indicates common enzymes identified in polysaccharides (common to avicel and xylan) but not in cellobiose.