Abstract：
:Saccharomyces cerevisiae grown on plastic surfaces formed organized structures, termed minicolonies, that consisted of a core of round (yeast-like) cells surrounded by chains of filamentous cells (pseudohyphae). Minicolonies had a much higher affinity for plastic than unstructured yeast communities growing on the same surface. Pseudohyphae at the surface of these colonies developed further into chains of asci. These structures suggest that pseudohyphal differentiation and sporulation are sequential processes in minicolonies. Consistent with this idea, minicolonies grown under conditions that stimulated pseudohyphal differentiation contained higher frequencies of asci. Furthermore, a flo11Δ mutant, which fails to form pseudohyphae, yielded normal sporulation in cultures, but was defective for minicolony sporulation. When minicolonies were dispersed in water and cells were then allowed to settle on the plastic surface, these cells sporulated very efficiently. Taken together, our results suggest that sporulation in minicolonies is stimulated by pseudohyphal differentiation because these pseudohyphae are dispersed from the core of the colony.
journal_name
FEMS Yeast Resjournal_title
FEMS yeast researchauthors
White MG,Piccirillo S,Dusevich V,Law DJ,Kapros T,Honigberg SMdoi
10.1111/j.1567-1364.2010.00712.xsubject
Has Abstractpub_date
2011-03-01 00:00:00pages
223-32issue
2eissn
1567-1356issn
1567-1364journal_volume
11pub_type
杂志文章abstract：:Mitogen activated protein kinase (MAPK) cascades are signal transduction mechanisms present in eukaryotic cells that allow adaptation to environmental changes. MAPK activity is mainly regulated by dual phosphorylation in a TXY motif present in the kinase subdomain VIII as well as dephosphorylation by specific phosphat...
journal_title：FEMS yeast research
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journal_title：FEMS yeast research
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journal_title：FEMS yeast research
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journal_title：FEMS yeast research
pub_type： 杂志文章,评审
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journal_title：FEMS yeast research
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journal_title：FEMS yeast research
pub_type： 杂志文章
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journal_title：FEMS yeast research
pub_type： 杂志文章
doi：10.1111/1567-1364.12086
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journal_title：FEMS yeast research
pub_type： 杂志文章
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更新日期：2005-04-01 00:00:00
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journal_title：FEMS yeast research
pub_type： 杂志文章
doi：10.1111/j.1567-1364.2006.00107.x
更新日期：2006-12-01 00:00:00
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journal_title：FEMS yeast research
pub_type： 杂志文章
doi：10.1093/femsyr/foz045
更新日期：2019-08-01 00:00:00
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journal_title：FEMS yeast research
pub_type： 杂志文章
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journal_title：FEMS yeast research
pub_type： 杂志文章
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更新日期：2009-02-01 00:00:00
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journal_title：FEMS yeast research
pub_type： 杂志文章
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更新日期：2011-12-01 00:00:00
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journal_title：FEMS yeast research
pub_type： 杂志文章
doi：10.1111/j.1567-1364.2008.00414.x
更新日期：2008-09-01 00:00:00
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journal_title：FEMS yeast research
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journal_title：FEMS yeast research
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journal_title：FEMS yeast research
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journal_title：FEMS yeast research
pub_type： 杂志文章
doi：10.1016/j.femsyr.2004.12.010
更新日期：2005-05-01 00:00:00
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journal_title：FEMS yeast research
pub_type： 杂志文章,评审
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更新日期：2006-03-01 00:00:00
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journal_title：FEMS yeast research
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journal_title：FEMS yeast research
pub_type： 杂志文章
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journal_title：FEMS yeast research
pub_type： 杂志文章
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更新日期：2004-05-01 00:00:00
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journal_title：FEMS yeast research
pub_type： 杂志文章,评审
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更新日期：2010-05-01 00:00:00
abstract：:Conversion of glucose to lactic acid is stoichiometrically equivalent to ethanol formation with respect to ATP formation from substrate-level phosphorylation, redox equivalents and product yield. However, anaerobic growth cannot be sustained in homolactate fermenting Saccharomyces cerevisiae. ATP-dependent export of t...
journal_title：FEMS yeast research
pub_type： 杂志文章
doi：10.1111/j.1567-1364.2009.00506.x
更新日期：2009-05-01 00:00:00
abstract：:d-Amino acid oxidase (DAO) is an important flavo-enzyme that catalyzes the oxidative deamination of d-amino acids into the corresponding alpha-keto acid, ammonia and H(2)O(2). We identified two amino acid oxidases in the methylotrophic yeast Pichia pastoris: Dao1p, which preferentially uses d-alanine as a substrate, a...
journal_title：FEMS yeast research
pub_type： 杂志文章
doi：10.1111/j.1567-1364.2010.00647.x
更新日期：2010-09-01 00:00:00
