Involvement of separate domains of the cellulosomal protein S1 of Clostridium thermocellum in binding to cellulose and in anchoring of catalytic subunits to the cellulosome

FEBS Letters

Béguin, Pierre¹  Tokatlidis, Kostas¹  Salamitou, Sylvie¹  Aubert, Jean-Paul¹ 

[1] Unité de Physiologie Cellulaire and URA 1300 CNRS, Département des Biotechnologies, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France

关键词: Cellulosome;    Scaffolding protein;    SI subunit;    Clostridium thermocellum;   

DOI  :  10.1016/0014-5793(92)80595-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Fragments of the 25OkDa SI subunit of the Clostridium thermocellum cellulosome were obtained by protease-induced or spontaneous degradation. All detectable fragments, down to a mass of about 30 kDa, retained the ability to bind to ¹²⁵I-labelled endoglucanase CelD, one of the catalytic subunits of the cellulosome. Several fragments were able to bind both to cellulose and to CElD. However, some fragments that could still bind to CelD did not have the ability to bind to cellulose. Therefore, S1, a putative scaffolding protein of the cellulosome, is likely to carry two separate types of domains, one of which binds to cellulose, while the other type binds to the various catalytic subunits of the complex.

【 授权许可】

Unknown