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ONLINEISSN:1347-6947
PRINTISSN:0916-8451
Bioscience, Biotechnology, and Biochemistry
Vol. 68 (2004) , No. 4 pp.924-926
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Interaction between a Type-II Dockerin Domain and a Type-II Cohesin Domain from Clostridium thermocellum Cellulosome
Sadanari JINDOU1), Tsutomu KAJINO2), Minoru INAGAKI1), Shuichi KARITA1), Pierre BEGUIN3), Tetsuya KIMURA1), Kazuo SAKKA1) and Kunio OHMIYA1)
1) Faculty of Bioresources, Mie University
2) Special Research Laboratory II, Toyota Central R&D Laboratories
3) Department of Biotechnology, Pasteur Institute
(Received September 24, 2003)
(Accepted November 21, 2003)
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 (KD) 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.
Key words:Clostridium thermocellum; cellulosome; dockerin; cohesin; surface plasmon resonance

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To cite this article:
Sadanari JINDOU, Tsutomu KAJINO, Minoru INAGAKI, Shuichi KARITA, Pierre BEGUIN, Tetsuya KIMURA, Kazuo SAKKA and Kunio OHMIYA, “Interaction between a Type-II Dockerin Domain and a Type-II Cohesin Domain from Clostridium thermocellum Cellulosome”, Biosci. Biotechnol. Biochem., Vol. 68, 924-926 (2004) .

doi:10.1271/bbb.68.924
JOI  JST.JSTAGE/bbb/68.924
Copyright (c) 2004 by Japan Society for Bioscience, Biotechnology, and Agrochemistry



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