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Title

The β-1,3-glucanosyltransferase gas4p is essential for ascospore wall maturation and spore viability in Schizosaccharomyces pombe

AuthorsMedina-Redondo, María de ; Arnáiz-Pita, Yolanda ; Rey Iglesias, Francisco del ; Vázquez de Aldana, Carlos R.
Issue Date8-Apr-2008
PublisherBlackwell Publishing
CitationMolecular Microbiology 68(5): 1283-1299 (2008)
AbstractMeiosis is the developmental programme by which sexually reproducing diploid organisms generate haploid gametes. In yeast, meiosis is followed by spore morphogenesis. The formation of the Schizosaccharomyces pombe ascospore wall requires the co-ordinated activity of enzymes involved in the biosynthesis and modification of its components, such as glucans. During sporogenesis, the β-1,3-glucan synthase bgs2p synthesizes linear β-1,3-glucans, which remain unorganized and alkali-soluble until covalent linkages are set up between β-1,3-glucans and other cell wall components. Several proteins belonging to the glycoside hydrolase family 72 (GH72) with β-1,3-glucanosyltransferase activity have been described in other organisms, such as the Saccharomyces cerevisiae Gas1p or the Aspergillus fumigatus Gel1p. Here we describe the characterization of gas4+, a new gene that encodes a protein of the GH72 family. Deletion of this gene does not lead to any apparent defect during vegetative growth, but homozygous gas4Δ diploids show a sporulation defect. Although meiosis occurs normally, ascospores are unable to mature or to germinate. The expression of gas4+ is strongly induced during sporulation and a yellow fluorescent protein (YFP)–gas4p fusion protein localizes to the ascospore periphery during sporulation. We conclude that gas4p is required for ascospore maturation in S. pombe.
Description17 pages, 8 figures.-- PMID: 18410286 [PubMed].-- Printed version published Jun 2008.-- et al.
Publisher version (URL)http://dx.doi.org/10.1111/j.1365-2958.2008.06233.x
URIhttp://hdl.handle.net/10261/10374
DOIhttp://dx.doi.org/10.1111/j.1365-2958.2008.06233.x
ISSN0950-382X
Appears in Collections:(IMB) Artículos
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