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 Martín, V.
Right arrow Articles by Sánchez, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Martín, V.
Right arrow Articles by Sánchez, Y.

 Previous Article  |  Next Article 

Eukaryotic Cell, February 2003, p. 159-169, Vol. 2, No. 1
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.1.159-169.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Bgs3p, a Putative 1,3-ß-Glucan Synthase Subunit, Is Required for Cell Wall Assembly in Schizosaccharomyces pombe

Victoria Martín, Blanca García, Elena Carnero, Angel Durán, and Yolanda Sánchez*

Instituto de Microbiología Bioquímica, CSIC/Universidad de Salamanca, and Departamento de Microbiología y Genética, Universidad de Salamanca, 37007 Salamanca, Spain

Received 31 July 2002/ Accepted 9 October 2002

ß-Glucans are the main components of the fungal cell wall. Fission yeast possesses a family of ß-glucan synthase-related genes. We describe here the cloning and characterization of bgs3+, a new member of this family. bgs3+ was cloned as a suppressor of a mutant hypersensitive to Echinocandin and Calcofluor White, drugs that interfere with cell wall biosynthesis. Disruption of the gene is lethal, and a decrease in Bgs3p levels leads to rounded cells with thicker walls, slightly reduces the amount of the ß-glucan, and raises the amount of {alpha}-glucan polymer. These cells finally died. bgs3+ is expressed in vegetative cells grown in different conditions and during mating and germination and is not enhanced by stress situations. Consistent with the observed expression pattern, Bgs3-green fluorescence protein (GFP-Bgs3p) was found at the growing tips during interphase and at the septum prior to cytokinesis, always localized to growth areas. We also found GFP-Bgs3p in mating projections, during the early stages of zygote formation, and at the growing pole during ascospore germination. We conclude that Bgs3p localization is restricted to growth areas and that Bgs3p is a glucan synthase homologue required for cell wall biosynthesis and cell elongation in the fission yeast life cycle.

* Corresponding author. Mailing address: Instituto de Microbiología Bioquímica, CSIC/Universidad de Salamanca, Edificio Departamental, Room 231, Campus Miguel de Unamuno, 37007 Salamanca, Spain. Phone: 34-923-121589. Fax: 34-923-224876. E-mail: ysm{at}usal.es.

Eukaryotic Cell, February 2003, p. 159-169, Vol. 2, No. 1
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.1.159-169.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Sharifmoghadam, M. R., Valdivieso, M.-H. (2009). The Fission Yeast SEL1 Domain Protein Cfh3p: A NOVEL REGULATOR OF THE GLUCAN SYNTHASE Bgs1p WHOSE FUNCTION IS MORE RELEVANT UNDER STRESS CONDITIONS. J. Biol. Chem. 284: 11070-11079 [Abstract] [Full Text]  
  • Garcia, P., Garcia, I., Marcos, F., de Garibay, G. R., Sanchez, Y. (2009). Fission Yeast Rgf2p Is a Rho1p Guanine Nucleotide Exchange Factor Required for Spore Wall Maturation and for the Maintenance of Cell Integrity in the Absence of Rgf1p. Genetics 181: 1321-1334 [Abstract] [Full Text]  
  • Ishihara, S., Hirata, A., Nogami, S., Beauvais, A., Latge, J.-P., Ohya, Y. (2007). Homologous Subunits of 1,3-Beta-Glucan Synthase Are Important for Spore Wall Assembly in Saccharomyces cerevisiae. Eukaryot Cell 6: 143-156 [Abstract] [Full Text]  
  • Lesage, G., Bussey, H. (2006). Cell Wall Assembly in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 70: 317-343 [Abstract] [Full Text]  
  • Hill, T. W., Loprete, D. M., Momany, M., Ha, Y., Harsch, L. M., Livesay, J. A., Mirchandani, A., Murdock, J. J., Vaughan, M. J., Watt, M. B. (2006). Isolation of cell wall mutants in Aspergillus nidulans by screening for hypersensitivity to Calcofluor White.. Mycologia 98: 399-409 [Abstract] [Full Text]  
  • Garcia, P., Tajadura, V., Garcia, I., Sanchez, Y. (2006). Rgf1p Is a Specific Rho1-GEF That Coordinates Cell Polarization with Cell Wall Biogenesis in Fission Yeast. Mol. Biol. Cell 17: 1620-1631 [Abstract] [Full Text]  
  • Morrell-Falvey, J. L., Ren, L., Feoktistova, A., Haese, G. D., Gould, K. L. (2005). Cell wall remodeling at the fission yeast cell division site requires the Rho-GEF Rgf3p. J. Cell Sci. 118: 5563-5573 [Abstract] [Full Text]  
  • Ge, W., Chew, T. G., Wachtler, V., Naqvi, S. N., Balasubramanian, M. K. (2005). The Novel Fission Yeast Protein Pal1p Interacts with Hip1-related Sla2p/End4p and Is Involved in Cellular Morphogenesis. Mol. Biol. Cell 16: 4124-4138 [Abstract] [Full Text]  
  • Cortes, J. C. G., Carnero, E., Ishiguro, J., Sanchez, Y., Duran, A., Ribas, J. C. (2005). The novel fission yeast (1,3){beta}-D-glucan synthase catalytic subunit Bgs4p is essential during both cytokinesis and polarized growth. J. Cell Sci. 118: 157-174 [Abstract] [Full Text]  
  • Tajadura, V., Garcia, B., Garcia, I., Garcia, P., Sanchez, Y. (2004). Schizosaccharomyces pombe Rgf3p is a specific Rho1 GEF that regulates cell wall {beta}-glucan biosynthesis through the GTPase Rho1p. J. Cell Sci. 117: 6163-6174 [Abstract] [Full Text]  
  • Cortes, J. C. G., Katoh-Fukui, R., Moto, K., Ribas, J. C., Ishiguro, J. (2004). Schizosaccharomyces pombe Pmr1p Is Essential for Cell Wall Integrity and Is Required for Polarized Cell Growth and Cytokinesis. Eukaryot Cell 3: 1124-1135 [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»