Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (16)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Kataeva, I. A.
Right arrow Articles by Ljungdahl, L. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kataeva, I. A.
Right arrow Articles by Ljungdahl, L. G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 14, No. 3, 167-172, March 2001
© 2001 Oxford University Press

Do domain interactions of glycosyl hydrolases from Clostridium thermocellum contribute to protein thermostability?

Irina A. Kataeva,1, David L. Blum,2, Xin-Liang Li and Lars G. Ljungdahl

Center for Biological Resources Recovery and Department of Biochemistry and Molecular Biology, A210 Life Sciences Building, University of Georgia, Athens, GA 30602-7229, USA

Cellulolytic and hemicellulolytic enzymes usually have a domain composition. The mutual influence of a cellulose-binding domain and a catalytic domain was investigated with cellobiohydrolase CelK and xylanase XynZ from Clostridium thermocellum. CelK is composed of an N-terminal family IV cellulose-binding domain (CBDIVCelK), a family 9 glycosyl hydrolase domain (Gh9CelK) and a dockerin domain (DD). CelK without the DD, (CBDIV–Gh9)CelK and CBDIVCelK bound cellulose. The thermostability of (CBDIV–Gh9)CelK was significantly higher than that of CBDIVCelK and Gh9CelK. The temperature optima of (CBDIV–Gh9)CelK and Gh9CelK were 65 and 45°C, respectively. XynZ consists of an N-terminal feruloyl esterase domain (FAEXynZ), a linker (L), a family VI CBD (CBDVIXynZ), a DD and a xylanase domain. FAEXynZ and (FAE–L–CBDVI)XynZ, used in the present study did not bind cellulose, but both were highly thermostable. Replacement of CBDVIXynZ with CBDIVCelK resulted in chimeras with feruloyl esterase activity and the ability to bind cellulose. CBDIVCelK–FAEXynZ bound cellulose with parameters similar to that of (CBDIV–Gh9)CelK. (FAE–L)XynZ–CBDIVCelK and FAEXynZ–CBDIVCelK had lower relative affinities and binding capacities than those of (CBDIV–Gh9)CelK. The three chimeras were much less thermostable than FAEXynZ and (FAE–L–CBDVI)XynZ. The results indicate that domains of glycosyl hydrolases are not randomly combined and that domain interactions affect properties of these domain-structured enzymes.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Protein Eng Des SelHome page
I. A. Kataeva, V. N. Uversky, J. M. Brewer, F. Schubot, J. P. Rose, B.-C. Wang, and L. G. Ljungdahl
Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA
Protein Eng. Des. Sel., November 1, 2004; 17(11): 759 - 769.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
T. Arai, R. Araki, A. Tanaka, S. Karita, T. Kimura, K. Sakka, and K. Ohmiya
Characterization of a Cellulase Containing a Family 30 Carbohydrate-Binding Module (CBM) Derived from Clostridium thermocellum CelJ: Importance of the CBM to Cellulose Hydrolysis
J. Bacteriol., January 15, 2003; 185(2): 504 - 512.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
I. A. Kataeva, R. D. Seidel III, A. Shah, L. T. West, X.-L. Li, and L. G. Ljungdahl
The Fibronectin Type 3-Like Repeat from the Clostridium thermocellum Cellobiohydrolase CbhA Promotes Hydrolysis of Cellulose by Modifying Its Surface
Appl. Envir. Microbiol., September 1, 2002; 68(9): 4292 - 4300.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.