Interaction between a Type-II Dockerin Domain and a Type-II Cohesin Domain from Clostridium thermocellum Cellulosome

• JINDOU Sadanari

  Faculty of Bioresources, Mie University

• KAJINO Tsutomu

  Special Research Laboratory II, Toyota Central R&D Laboratories

• INAGAKI Minoru

  Faculty of Bioresources, Mie University

• KARITA Shuichi

  Faculty of Bioresources, Mie University

• BEGUIN Pierre

  Department of Biotechnology, Pasteur Institute

• KIMURA Tetsuya

  Faculty of Bioresources, Mie University

• SAKKA Kazuo

  Faculty of Bioresources, Mie University

• OHMIYA Kunio

  Faculty of Bioresources, Mie University

Bibliographic Information

Other Title

• Interaction between a Type-2 Dockerin Domain and a Type-2 Cohesin Domain from Clostridium thermocellum Cellulosome
• Interaction between a Type-II Dockerin Domain and a Type-II Cohesin Domain from<i>Clostridium thermocellum</i>Cellulosome

Abstract

The interaction between the type-II dockerin domain of the scaffoldin protein CipA and the type-II cohesin domain of the outer layer protein SdbA is the fundamental mechanism for anchoring the cellulosome to the cell surface of Clostridium thermocellum. We constructed and purified a dockerin polypeptide and a cohesin polypeptide, and determined affinity constants of the interaction between them by the surface plasmon resonance method. The dissociation constant (K_D) value was 1.8×10⁻⁹ M, which is a little larger than that for the combination of a type-I dockerin and a type-I cohesin.

Journal

• Bioscience, Biotechnology, and Biochemistry

  Bioscience, Biotechnology, and Biochemistry 68 (4), 924-926, 2004

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• <I>Clostridium thermocellum</I>
• cellulosome
• dockerin
• cohesin
• surface plasmon resonance

Details

• CRID: 1390282681450474624
• NII Article ID: 10013144102
• NII Book ID: AA10824164
• DOI: 10.1271/bbb.68.924
• COI: 1:CAS:528:DC%2BD2cXjvFersLw%3D
• ISSN: 13476947
• ISSN: 09168451
• NDL BIB ID: 6930460
• PubMed: 15118324
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I6930460
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.68.924
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
• Abstract License Flag: Disallowed