JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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 Schmitt, M. P.
Right arrow Articles by Drazek, E. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schmitt, M. P.
Right arrow Articles by Drazek, E. S.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 2001, p. 1476-1481, Vol. 183, No. 4
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.4.1476-1481.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Construction and Consequences of Directed Mutations Affecting the Hemin Receptor in Pathogenic Corynebacterium Species

Michael P. Schmitt* and E. Susan Drazek

Laboratory of Bacterial Toxins, Division of Bacterial, Allergenic and Parasitic Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892

Received 15 September 2000/Accepted 26 November 2000

Genes encoding an ATP-binding cassette transporter system involved in hemin iron utilization from Corynebacterium ulcerans were cloned and characterized. The genes are homologous to a hemin transport system previously identified in Corynebacterium diphtheriae. Disruption of the hmuT gene, which encodes the putative hemin receptor, resulted in greatly reduced ability of C. ulcerans to use hemin or hemoglobin as an iron source. Inactivation of hmuT in C. diphtheriae by site-specific recombination had no effect on hemin utilization, which suggests that C. diphtheriae has an additional system for transporting hemin.


* Corresponding author. Mailing address: FDA/CBER/DBPAP, 8800 Rockville Pike, Bldg. 29, Room 108, Bethesda, MD 20892. E-mail: schmitt{at}cber.fda.gov. Phone: (301) 435-2424. Fax: (301) 402-2776.


Journal of Bacteriology, February 2001, p. 1476-1481, Vol. 183, No. 4
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.4.1476-1481.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:




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 © 2001 by the American Society for Microbiology. All rights reserved.