Acetyltransferase SAS2 and sirtuin SIR2, respectively, control flocculation and biofilm formation in wine yeast. Issue 6 (26th June 2014)
- Record Type:
- Journal Article
- Title:
- Acetyltransferase SAS2 and sirtuin SIR2, respectively, control flocculation and biofilm formation in wine yeast. Issue 6 (26th June 2014)
- Main Title:
- Acetyltransferase SAS2 and sirtuin SIR2, respectively, control flocculation and biofilm formation in wine yeast
- Authors:
- Rodriguez, María E.
Orozco, Helena
Cantoral, Jesús M.
Matallana, Emilia
Aranda, Agustín - Abstract:
- <abstract abstract-type="main" id="fyr12173-abs-0001"> <title>Abstract</title> <p>Cell‐to‐cell and cell‐to‐environment interactions of microorganisms are of substantial relevance for their biotechnological use. In the yeast <italic>Saccharomyces cerevisiae</italic>, flocculation can be an advantage to clarify final liquid products after fermentation, and biofilm formation may be relevant for the encapsulation of strains of interest. The adhesion properties of wine yeast strains can be modified by the genetic manipulation of transcriptional regulatory proteins, such as histone deacetylases, and acetylases. Sirtuin <italic>SIR2</italic> is essential for the formation of mat structures, a kind of biofilm that requires the expression of cell‐wall protein <italic>FLO11</italic> as its deletion reduces <italic>FLO11</italic> expression, and adhesion of cells to themselves and to agar in a commercial wine strain. Deletion of acetyltransferase <italic>GCN5</italic> leads to a similar phenotype. A naturally flocculant wine yeast strain called P2 was characterized. Its flocculation happens only during grape juice fermentation and is due to the presence of a highly transcribed version of flocculin <italic>FLO5, </italic> linked to the presence of a δ sequence in the promoter. Deletion of acetyltransferase <italic>SAS2</italic> enhances this phenotype and maltose fermentation even more. Therefore, the manipulation of acetylation/deacetylation machinery members is a valid way to alter<abstract abstract-type="main" id="fyr12173-abs-0001"> <title>Abstract</title> <p>Cell‐to‐cell and cell‐to‐environment interactions of microorganisms are of substantial relevance for their biotechnological use. In the yeast <italic>Saccharomyces cerevisiae</italic>, flocculation can be an advantage to clarify final liquid products after fermentation, and biofilm formation may be relevant for the encapsulation of strains of interest. The adhesion properties of wine yeast strains can be modified by the genetic manipulation of transcriptional regulatory proteins, such as histone deacetylases, and acetylases. Sirtuin <italic>SIR2</italic> is essential for the formation of mat structures, a kind of biofilm that requires the expression of cell‐wall protein <italic>FLO11</italic> as its deletion reduces <italic>FLO11</italic> expression, and adhesion of cells to themselves and to agar in a commercial wine strain. Deletion of acetyltransferase <italic>GCN5</italic> leads to a similar phenotype. A naturally flocculant wine yeast strain called P2 was characterized. Its flocculation happens only during grape juice fermentation and is due to the presence of a highly transcribed version of flocculin <italic>FLO5, </italic> linked to the presence of a δ sequence in the promoter. Deletion of acetyltransferase <italic>SAS2</italic> enhances this phenotype and maltose fermentation even more. Therefore, the manipulation of acetylation/deacetylation machinery members is a valid way to alter the interaction of industrial yeast to their environment.</p> </abstract> … (more)
- Is Part Of:
- FEMS yeast research. Volume 14:Issue 6(2014)
- Journal:
- FEMS yeast research
- Issue:
- Volume 14:Issue 6(2014)
- Issue Display:
- Volume 14, Issue 6 (2014)
- Year:
- 2014
- Volume:
- 14
- Issue:
- 6
- Issue Sort Value:
- 2014-0014-0006-0000
- Page Start:
- 845
- Page End:
- 857
- Publication Date:
- 2014-06-26
- Subjects:
- Yeast -- Periodicals
Yeasts -- Periodicals
579.562 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1567-1364 ↗
http://www.sciencedirect.com/science/journal/15671356 ↗
http://www.blackwell-synergy.com/rd.asp?goto=journal&code=fyr ↗
http://onlinelibrary.wiley.com/ ↗
http://femsyr.oxfordjournals.org/content/ ↗ - DOI:
- 10.1111/1567-1364.12173 ↗
- Languages:
- English
- ISSNs:
- 1567-1356
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.325000
British Library DSC - BLDSS-3PM
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- 3855.xml