This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Reeves, R. A.
Right arrow Articles by Bergquist, P. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Reeves, R. A.
Right arrow Articles by Bergquist, P. L.
Agricola
Right arrow Articles by Reeves, R. A.
Right arrow Articles by Bergquist, P. L.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, April 2000, p. 1532-1537, Vol. 66, No. 4
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Sequencing and Expression of Additional Xylanase Genes from the Hyperthermophile Thermotoga maritima FjSS3B.1

Rosalind A. Reeves,1 Moreland D. Gibbs,1 Daniel D. Morris,1 Katherine R. Griffiths,1 David J. Saul,2 and Peter L. Bergquist1,3,*

Department of Biological Sciences, Macquarie University, Sydney New South Wales, Australia,1 and Centre for Gene Technology, University of Auckland,2 and Department of Molecular Medicine, University of Auckland Medical School,3 Auckland, New Zealand

Received 19 October 1999/Accepted 10 January 2000

Two genes, xynB and xynC, coding for xylanases were isolated from Thermotoga maritima FjSS3B.1 by a genomic-walking-PCR technique. Sequencing of the genes showed that they encode multidomain family 10 xylanases. Only XynB exhibited activity against xylan substrates. The temperature optimum (87°C) and pH optimum (pH 6.5) of XynB are different from the previously reported xylanase, XynA (also a family 10 enzyme), from this organism. The catalytic domain expressed without other domains has a lower temperature optimum, is less thermostable, and has optimal activity at pH 6.5. Despite having a high level of sequence similarity to xynB, xynC appears to be nonfunctional since its encoded protein did not show significant activity on xylan substrates.


* Corresponding author. Mailing address: Research Office, Macquarie University, Sydney, NSW 2109, Australia. Phone: 61-2-9850-8614. Fax: 61-2-9850-8799. E-mail: peter.bergquist{at}mq.edu.au.


Applied and Environmental Microbiology, April 2000, p. 1532-1537, Vol. 66, No. 4
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Kataeva, I. A., Uversky, V. N., Brewer, J. M., Schubot, F., Rose, J. P., Wang, B.-C., Ljungdahl, L. G. (2004). Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA. Protein Eng Des Sel 17: 759-769 [Abstract] [Full Text]  
  • Lee, D.-W., Jang, H.-J., Choe, E.-A., Kim, B.-C., Lee, S.-J., Kim, S.-B., Hong, Y.-H., Pyun, Y.-R. (2004). Characterization of a Thermostable L-Arabinose (D-Galactose) Isomerase from the Hyperthermophilic Eubacterium Thermotoga maritima. Appl. Environ. Microbiol. 70: 1397-1404 [Abstract] [Full Text]  
  • Nesbo, C. L., Nelson, K. E., Doolittle, W. F. (2002). Suppressive Subtractive Hybridization Detects Extensive Genomic Diversity in Thermotoga maritima. J. Bacteriol. 184: 4475-4488 [Abstract] [Full Text]  
  • Suzuki, M., Kato, A., Nagata, N., Komeda, Y. (2002). A Xylanase, AtXyn1, is Predominantly Expressed in Vascular Bundles, and Four Putative Xylanase Genes were Identified in the Arabidopsis thaliana Genome. Plant Cell Physiol 43: 759-767 [Abstract] [Full Text]  
  • Nesb, C. L., L'Haridon, S., Stetter, K. O., Doolittle, W. F. (2001). Phylogenetic Analyses of Two "Archaeal" Genes in Thermotoga maritima Reveal Multiple Transfers Between Archaea and Bacteria. Mol Biol Evol 18: 362-375 [Abstract] [Full Text]  
  • Sunna, A., Gibbs, M. D., Bergquist, P. L. (2000). A novel thermostable multidomain 1,4-{beta}-xylanase from 'Caldibacillus cellulovorans' and effect of its xylan-binding domain on enzyme activity. Microbiology 146: 2947-2955 [Abstract] [Full Text]