Premium
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
Author(s) -
Salamitou Sylvie,
Tokatlidis Kostas,
Béguin Pierre,
Aubert Jean-Paul
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80595-8
Subject(s) - cellulosome , clostridium thermocellum , cellulose , chemistry , biochemistry , anchoring , catalysis , protein subunit , cellulase , gene , structural engineering , engineering
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 125 I‐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.