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 Park, Y.
Right arrow Articles by Park, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Park, Y.
Right arrow Articles by Park, C.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 1999, p. 1039-1042, Vol. 181, No. 3
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Topology of RbsC, a Membrane Component of the Ribose Transporter, Belonging to the AraH Superfamily

Yongkyu Park and Chankyu Park*

National Creative Research Initiative Center for Behavioral Genetics, Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Yusong-Ku, Taejon, Republic of Korea

Received 14 September 1998/Accepted 9 November 1998

RbsC of Escherichia coli is the hydrophobic membrane component of ribose uptake system classified as the ATP-binding cassette transporter. To understand the structure and function of RbsC, its transmembrane topology was investigated by using 64 RbsC-PhoA fusions isolated either specifically or randomly. In order to confirm the cytoplasmic location of the short C-terminal region (5 amino acids), inside-out or right-side-out membrane vesicles were generated, and the C-terminal region was found to be digested by carboxypeptidase A only in inside-out vesicles. This result is consistent with the model, based on the results of alkaline phosphatase fusions, in which the protein traverses the membrane six times and the N and C termini are exposed to the cytoplasm.


* Corresponding author. Mailing address: National Creative Research Initiative Center for Behavioral Genetics, Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Yusong-Ku, Taejon, Republic of Korea. Phone: 82-42-869-2629. Fax: 82-42-869-2610. E-mail: ckpark{at}hanbit.kaist.ac.kr.


Journal of Bacteriology, February 1999, p. 1039-1042, Vol. 181, No. 3
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Tomasinsig, L., Scocchi, M., Mettulio, R., Zanetti, M. (2004). Genome-Wide Transcriptional Profiling of the Escherichia coli Response to a Proline-Rich Antimicrobial Peptide. Antimicrob. Agents Chemother. 48: 3260-3267 [Abstract] [Full Text]  
  • Stewart, J. B., Hermodson, M. A. (2003). Topology of RbsC, the Membrane Component of the Escherichia coli Ribose Transporter. J. Bacteriol. 185: 5234-5239 [Abstract] [Full Text]  
  • Ouchane, S., Kaplan, S. (1999). Topological Analysis of the Membrane-localized Redox-responsive Sensor Kinase PrrB from Rhodobacter sphaeroides 2.4.1. J. Biol. Chem. 274: 17290-17296 [Abstract] [Full Text]