Eukaryotic Cell
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF 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 Oberholzer, U.
Right arrow Articles by Whiteway, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Oberholzer, U.
Right arrow Articles by Whiteway, M.

 Previous Article  |  Next Article 

Eukaryotic Cell, April 2002, p. 213-228, Vol. 1, No. 2
1535-9778/02/$04.00+0     DOI: 10.1128/EC.1.2.213-228.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Myosin I Is Required for Hypha Formation in Candida albicans{dagger}

U. Oberholzer,1* A. Marcil,1 E. Leberer,2,{ddagger} D. Y. Thomas,3,4,§ and M. Whiteway1,3

Genetics Division, Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec H4P 2R2,1 Departments of Biology,3 Anatomy and Cell Biology,4 Experimental Medicine, McGill University, Montreal, Quebec H3A 2B2, Canada2

Received 30 July 2001/ Accepted 3 January 2002

The pathogenic yeast Candida albicans can undergo a dramatic change in morphology from round yeast cells to long filamentous cells called hyphae. We have cloned the CaMYO5 gene encoding the only myosin I in C. albicans. A strain with a deletion of both copies of CaMYO5 is viable but cannot form hyphae under all hypha-inducing conditions tested. This mutant exhibits a higher frequency of random budding and a depolarized distribution of cortical actin patches relative to the wild-type strain. We found that polar budding, polarized localization of cortical actin patches, and hypha formation are dependent on a specific phosphorylation site on myosin I, called the "TEDS-rule" site. Mutation of this serine 366 to alanine gives rise to the null mutant phenotype, while a S366D mutation, the product of which mimics a phosphorylated serine, allows hypha formation. However, the S366D mutation still causes a depolarized distribution of cortical actin patches in budding cells, similar to that in the null mutant. The localization of CaMyo5-GFP together with cortical actin patches at the bud and hyphal tips is also dependent on serine 366. Intriguingly, the cortical actin patches in the majority of the hyphae of the mutant expressing Camyo5S366D were depolarized, suggesting that although their distribution is dependent on myosin I localization, polarized cortical actin patches may not be required for hypha formation.

* Corresponding author. Mailing address: Genetics Division, Biotechnology Research Institute, 6100 Royalmount, Montreal, Quebec H4P 2R2, Canada. Phone: (514) 496-6358. Fax: (514) 496-6213. E-mail: ursula.oberholzer{at}nrc.ca.

{dagger} NRCC publication 44811.

{ddagger} Present address: Aventis Genomics Center, Aventis Pharma, Martinsried D-82152, Germany.

§ Present address: Chair of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada.

Eukaryotic Cell, April 2002, p. 213-228, Vol. 1, No. 2
1535-9778/02/$04.00+0     DOI: 10.1128/EC.1.2.213-228.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Appl. Environ. Microbiol. Infect. Immun. J. Bacteriol.
Mol. Cell Biol. Microbiol. Mol. Biol. Rev. ALL ASM JOURNALS
Copyright © 2002 by the American Society for Microbiology.