Nonproteolytic cleavage of aspartyl proline bonds in the cellulosomal scaffoldin subunit from Clostridium thermocellum |
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| Authors: | Raphael Lamed Rina Kenig Ely Morag Sima Yaron Yuval Shoham Edward A Bayer |
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| Institution: | (1) Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Israel;(2) Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel;(3) Department of Food Engineering and Biotechnology, Technion—Israel Institute of Technology, Haifa, Israel |
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| Abstract: | Previous work from our group Morag (Morgenstern), E., Bayer, E. A., and Lamed, R. (1991), Appl. Biochem. Biotechnol.
30, 129–136] has demonstrated an anomalous electrophoretic mobility pattern for scaffoldin, the 210-kDa cellulosome-integrating
subunit of Clostridium thermocellum. Subsequent evidence Morag, E., Bayer, E. A., and Lamed, R. (1992), Appl. Biochem. Biotechnol.
33, 205–217] indicated that the effect could be attributed to a nonproteolytic fragmentation of the subunit into a defined series
of lowermolecular-weight bands. In the present work, a recombinant segment of the scaffoldin subunit was employed to determine
the site(s) of bond breakage. An Asp-Pro sequence within the cohesin domain was identified to be the sensitive peptide bond.
This sequence appears quite frequently in the large cellulosomal proteins, and the labile bond may be related to an as yet
undescribed physiological role in the hydrolysis of cellulose by cellulosomes. |
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| Keywords: | Cellulosome multienzyme complex cohesin domain Asp-Pro bond cellulases Clostridium thermocellum |
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