Document Detail


Thermal unfolding and modular architecture of Clostridium stercorarium Xyn10B.
MedLine Citation:
PMID:  17485827     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
To examine the possibility of module interaction in the thermal unfolding of different modular architectures, four truncated proteins were constructed from Clostridium stercorarium Xyn10B: a family 10 catalytic module (CM10), a polypeptide compound of one family 22 carbohydrate-binding module (CBM22-2) and the catalytic module (CBM22-CM10), two family 22 CBMs and the catalytic module (2CBM22-CM10), and only two family 22 CBMs (2CBM22). Thermal unfolding of four proteins were observed by differential scanning calorimetry. CM10 was unfolded reversibly and denatured as one component. The unfolding of protein CBM22-CM10 comprising CBM22-2 connected with CM10 was irreversible, and can be assumed to be one-component denaturation. Protein 2CBM22, with two CBM22s in tandem, unfolded as two independent modules. However, 2CBM22-CM10, with two CBM22s, unfolded as two and not the expected three separate components. These findings constitute the first reported case in which differences in thermal unfolding units and mechanisms were derived from differences in the modular architectures of proteins.
Authors:
Rie Araki; Shuichi Karita; Akiyoshi Tanaka; Miki Suzuki; Tetsuya Kimura; Kazuo Sakka
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Publication Detail:
Type:  Journal Article     Date:  2007-05-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  71     ISSN:  0916-8451     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2007 May 
Date Detail:
Created Date:  2007-05-23     Completed Date:  2007-07-05     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  1322-6     Citation Subset:  IM    
Affiliation:
Sustainable Resource Sciences, Graduate School of Bioresources, Mie University, Tsu, Japan.
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MeSH Terms
Descriptor/Qualifier:
Calorimetry, Differential Scanning
Carbohydrate Metabolism
Catalysis
Clostridium / enzymology*
Endo-1,4-beta Xylanases / chemistry,  genetics,  metabolism*
Hydrogen-Ion Concentration
Protein Denaturation*
Recombinant Proteins / chemistry,  isolation & purification,  metabolism
Temperature
Thermodynamics
Chemical
Reg. No./Substance:
0/Recombinant Proteins; EC 3.2.1.8/Endo-1,4-beta Xylanases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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