JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
JB.00584-07v1
189/17/6260    most recent
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 Google Scholar
Google Scholar
Right arrow Articles by Chen, S.
Right arrow Articles by Wilson, D. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chen, S.
Right arrow Articles by Wilson, D. B.
Journal of Bacteriology, September 2007, p. 6260-6265, Vol. 189, No. 17
0021-9193/07/$08.00+0     doi:10.1128/JB.00584-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Proteomic and Transcriptomic Analysis of Extracellular Proteins and mRNA Levels in Thermobifida fusca Grown on Cellobiose and Glucose{triangledown}

Shaolin Chen{dagger} and David B. Wilson*

Department of Molecular Biology and Genetics, 458 Biotechnology Building, Cornell University, Ithaca, New York 14853

Received 16 April 2007/ Accepted 19 June 2007

Thermobifida fusca secretes proteins that carry out plant cell wall degradation. Using two-dimensional electrophoresis, the extracellular proteome of T. fusca grown on cellobiose was compared to that of cells grown on glucose. Extracellular proteins, the expression of which is induced by cellobiose, mainly are cellulases and cellulose-binding proteins. Other major extracellular proteins induced by cellobiose include a xylanase (Xyl10A) and two unknown proteins, the C-terminal regions of which are homologous to a lytic transglycosylase goose egg white lysozyme domain and an NLPC_P60 domain (which defines a family of cell wall peptidases), respectively. Transcriptional analysis of genes encoding cellobiose-induced proteins suggests that their expression is controlled at the transcriptional level and that their expression also is induced by cellulose. Some other major extracellular proteins produced by T. fusca grown on both cellobiose and glucose include Lam81A and three unknown proteins that are homologous to aminopeptidases and xylanases or that contain a putative NLPC_P60 domain.


* Corresponding author. Mailing address: Department of Molecular Biology and Genetics, 458 Biotechnology Building, Cornell University, Ithaca, NY 14853. Phone: (607) 255-5706. Fax: (607) 255-2436. E-mail: dbw3{at}cornell.edu

{triangledown} Published ahead of print on 29 June 2007.

{dagger} Present address: Department of Plant Biology, Carnegie Institution of Washington, Stanford, CA 94305.


Journal of Bacteriology, September 2007, p. 6260-6265, Vol. 189, No. 17
0021-9193/07/$08.00+0     doi:10.1128/JB.00584-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2007 by the American Society for Microbiology. All rights reserved.