This Article
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 Lytle, B.
Right arrow Articles by Wu, J. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lytle, B.
Right arrow Articles by Wu, J. H.

 Previous Article  |  Next Article 

J. Bacteriol., 02 1996, 1200-1203, Vol 178, No. 4
Copyright © 1996, American Society for Microbiology

Interactions of the CelS binding ligand with various receptor domains of the Clostridium thermocellum cellulosomal scaffolding protein, CipA

B Lytle, C Myers, K Kruus and JH Wu
Department of Chemical Engineering, University of Rochester, New York 14627-0166, USA.

The Clostridium thermocellum cellulosomal scaffolding protein, CipA, acts as an anchor on the cellulose surface for the various catalytic subunits of the cellulosome, a large extracellular cellulase complex. CipA contains nine repeated domains that serve as receptors for the cellulosomal catalytic subunits, each of which carries a conserved, duplicated ligand sequence (DS). Four representative CipA receptor domains with sequence dissimilarity were cloned and expressed in Escherichia coli. The interaction of these cloned receptor domains with the duplicated ligand sequence of CelS (expressed as a thioredoxin fusion protein, TRX-DSCelS), was studied by nondenaturing polyacrylamide gel electrophoresis. TRX-DSCelS formed a stable complex with each of the four receptor domains, indicating that CelS, the most abundant cellulosomal catalytic subunit, binds nonselectively to all of the CipA receptors. Conversely, the duplicated sequence of CipA (in the form of TRX-DSCipA), which is homologous to that of CelS, did not bind to any of the receptors under the experimental conditions.


This article has been cited by other articles:

  • Carvalho, A. L., Dias, F. M. V., Nagy, T., Prates, J. A. M., Proctor, M. R., Smith, N., Bayer, E. A., Davies, G. J., Ferreira, L. M. A., Romao, M. J., Fontes, C. M. G. A., Gilbert, H. J. (2007). Evidence for a dual binding mode of dockerin modules to cohesins. Proc. Natl. Acad. Sci. USA 104: 3089-3094 [Abstract] [Full Text]  
  • Demain, A. L., Newcomb, M., Wu, J. H. D. (2005). Cellulase, Clostridia, and Ethanol. Microbiol. Mol. Biol. Rev. 69: 124-154 [Abstract] [Full Text]  
  • Nakar, D., Handelsman, T., Shoham, Y., Fierobe, H.-P., Belaich, J.-P., Morag, E., Lamed, R., Bayer, E. A. (2004). Pinpoint Mapping of Recognition Residues on the Cohesin Surface by Progressive Homologue Swapping. J. Biol. Chem. 279: 42881-42888 [Abstract] [Full Text]  
  • Jindou, S., Soda, A., Karita, S., Kajino, T., Beguin, P., Wu, J. H. D., Inagaki, M., Kimura, T., Sakka, K., Ohmiya, K. (2004). Cohesin-Dockerin Interactions within and between Clostridium josui and Clostridium thermocellum: BINDING SELECTIVITY BETWEEN COGNATE DOCKERIN AND COHESIN DOMAINS AND SPECIES SPECIFICITY. J. Biol. Chem. 279: 9867-9874 [Abstract] [Full Text]  
  • Carvalho, A. L., Dias, F. M. V., Prates, J. A. M., Nagy, T., Gilbert, H. J., Davies, G. J., Ferreira, L. M. A., Romao, M. J., Fontes, C. M. G. A. (2003). Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex. Proc. Natl. Acad. Sci. USA 100: 13809-13814 [Abstract] [Full Text]  
  • Kataeva, I., Li, X.-L., Chen, H., Choi, S.-K., Ljungdahl, L. G. (1999). Cloning and Sequence Analysis of a New Cellulase Gene Encoding CelK, a Major Cellulosome Component of Clostridium thermocellum: Evidence for Gene Duplication and Recombination. J. Bacteriol. 181: 5288-5295 [Abstract] [Full Text]  
  • Pagès, S., Bélaïch, A., Fierobe, H.-P., Tardif, C., Gaudin, C., Bélaïch, J.-P. (1999). Sequence Analysis of Scaffolding Protein CipC and ORFXp, a New Cohesin-Containing Protein in Clostridium cellulolyticum: Comparison of Various Cohesin Domains and Subcellular Localization of ORFXp. J. Bacteriol. 181: 1801-1810 [Abstract] [Full Text]  
  • Lytle, B., Wu, J. H. D. (1998). Involvement of Both Dockerin Subdomains in Assembly of the Clostridium thermocellum Cellulosome. J. Bacteriol. 180: 6581-6585 [Abstract] [Full Text]  
  • Zverlov, V. V., Velikodvorskaya, G. V., Schwarz, W. H., Bronnenmeier, K., Kellermann, J., Staudenbauer, W. L. (1998). . J. Bacteriol. 180: 3091-3099 [Abstract] [Full Text]  
  • Mechaly, A., Fierobe, H.-P., Belaich, A., Belaich, J.-P., Lamed, R., Shoham, Y., Bayer, E. A. (2001). Cohesin-Dockerin Interaction in Cellulosome Assembly. A SINGLE HYDROXYL GROUP OF A DOCKERIN DOMAIN DISTINGUISHES BETWEEN NONRECOGNITION AND HIGH AFFINITY RECOGNITION. J. Biol. Chem. 276: 9883-9888 [Abstract] [Full Text]  
  • Fierobe, H.-P., Mechaly, A., Tardif, C., Belaich, A., Lamed, R., Shoham, Y., Belaich, J.-P., Bayer, E. A. (2001). Design and Production of Active Cellulosome Chimeras. SELECTIVE INCORPORATION OF DOCKERIN-CONTAINING ENZYMES INTO DEFINED FUNCTIONAL COMPLEXES. J. Biol. Chem. 276: 21257-21261 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»