| Unusual binding properties of the dockerin module of Clostridium thermocellum endoglucanase CelJ (Cel9D-Cel44A). | |
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MedLine Citation:
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PMID: 19811541 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Cellulosomes are cellulolytic complexes produced by anaerobic bacteria, and are composed of a scaffolding protein and several catalytic components. The complexes are formed by highly specific interactions of one of the reiterated cohesin modules of the scaffolding protein with a dockerin module of the catalytic components. The affinities of a dockerin module of Clostridium thermocellum CelJ (Cel9D-Cel44A) for several cohesin modules from C. thermocellum and Clostridium josui scaffolding proteins were quantitatively measured by surface plasmon resonance analysis. The recombinant CelJ dockerin-containing protein interacted with three recombinant C. josui cohesin proteins as well as recombinant C. thermocellum cohesin proteins beyond the so-called 'species specificity' of the dockerin and cohesin interactions. However, this protein did not recognize a second cohesin module from the C. josui scaffolding protein, suggesting that the catalytic components are not necessarily arranged randomly on a scaffolding protein in native cellulosomes. |
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Authors:
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Kazutaka Sakka; Yuko Kishino; Yuka Sugihara; Sadanari Jindou; Makiko Sakka; Minoru Inagaki; Tetsuya Kimura; Kazuo Sakka |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2009-09-10 |
Journal Detail:
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Title: FEMS microbiology letters Volume: 300 ISSN: 1574-6968 ISO Abbreviation: FEMS Microbiol. Lett. Publication Date: 2009 Nov |
Date Detail:
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Created Date: 2009-10-23 Completed Date: 2009-12-16 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7705721 Medline TA: FEMS Microbiol Lett Country: England |
Other Details:
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Languages: eng Pagination: 249-55 Citation Subset: IM |
Affiliation:
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Graduate School of Bioresources, Mie University, Tsu, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Bacterial Proteins / metabolism* Carrier Proteins / metabolism Cell Cycle Proteins / metabolism Cellulase / metabolism* Chromosomal Proteins, Non-Histone / metabolism Clostridium thermocellum / enzymology* Molecular Sequence Data Phylogeny Protein Binding Sequence Homology, Amino Acid Surface Plasmon Resonance |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Carrier Proteins; 0/Cell Cycle Proteins; 0/Chromosomal Proteins, Non-Histone; 0/cohesins; 147258-12-6/cellulose binding protein A, Clostridium cellulovorans; EC 3.2.1.4/CelJ protein, Clostridium thermocellum; EC 3.2.1.4/Cellulase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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