The conserved histone deacetylase Rpd3 and the DNA binding regulator Ume6 repress BOI1's meiotic transcript isoform during vegetative growth in Saccharomyces cerevisiae. Issue 4 (21st March 2015)
- Record Type:
- Journal Article
- Title:
- The conserved histone deacetylase Rpd3 and the DNA binding regulator Ume6 repress BOI1's meiotic transcript isoform during vegetative growth in Saccharomyces cerevisiae. Issue 4 (21st March 2015)
- Main Title:
- The conserved histone deacetylase Rpd3 and the DNA binding regulator Ume6 repress BOI1's meiotic transcript isoform during vegetative growth in Saccharomyces cerevisiae
- Authors:
- Liu, Yuchen
Stuparevic, Igor
Xie, Bingning
Becker, Emmanuelle
Law, Michael J.
Primig, Michael - Abstract:
- <abstract abstract-type="main"> <title>Summary</title> <p> <italic>BOI</italic> <italic>1</italic> and <italic>BOI</italic><italic>2</italic> are paralogs important for the actin cytoskeleton and polar growth. <italic>BOI</italic><italic>1</italic> encodes a meiotic transcript isoform with an extended 5′‐untranslated region predicted to impair protein translation. It is, however, unknown how the isoform is repressed during mitosis, and if Boi1 is present during sporulation. By interpreting microarray data from <italic>MAT</italic>a cells, <italic>MAT</italic>a/α cells, a starving <italic>MAT</italic>α/α control, and a meiosis‐impaired <italic>rrp6</italic> mutant, we classified <italic>BOI</italic><italic>1</italic>'s extended isoform as early meiosis‐specific. These results were confirmed by RNA‐Sequencing, and extended by a 5′‐RACE assay and Northern blotting, showing that meiotic cells induce the long isoform while the mitotic isoform remains detectable during meiosis. We provide evidence via motif predictions, an <italic>in vivo</italic> binding assay and genetic experiments that the Rpd3/Sin3/Ume6 histone deacetylase complex, which represses meiotic genes during mitosis, also prevents the induction of <italic>BOI</italic><italic>1</italic>'s 5′‐extended isoform in mitosis by direct binding of Ume6 to its URS1 target. Finally, we find that Boi1 protein levels decline when cells switch from fermentation to respiration and sporulation. The histone deacetylase Rpd3 is<abstract abstract-type="main"> <title>Summary</title> <p> <italic>BOI</italic> <italic>1</italic> and <italic>BOI</italic><italic>2</italic> are paralogs important for the actin cytoskeleton and polar growth. <italic>BOI</italic><italic>1</italic> encodes a meiotic transcript isoform with an extended 5′‐untranslated region predicted to impair protein translation. It is, however, unknown how the isoform is repressed during mitosis, and if Boi1 is present during sporulation. By interpreting microarray data from <italic>MAT</italic>a cells, <italic>MAT</italic>a/α cells, a starving <italic>MAT</italic>α/α control, and a meiosis‐impaired <italic>rrp6</italic> mutant, we classified <italic>BOI</italic><italic>1</italic>'s extended isoform as early meiosis‐specific. These results were confirmed by RNA‐Sequencing, and extended by a 5′‐RACE assay and Northern blotting, showing that meiotic cells induce the long isoform while the mitotic isoform remains detectable during meiosis. We provide evidence via motif predictions, an <italic>in vivo</italic> binding assay and genetic experiments that the Rpd3/Sin3/Ume6 histone deacetylase complex, which represses meiotic genes during mitosis, also prevents the induction of <italic>BOI</italic><italic>1</italic>'s 5′‐extended isoform in mitosis by direct binding of Ume6 to its URS1 target. Finally, we find that Boi1 protein levels decline when cells switch from fermentation to respiration and sporulation. The histone deacetylase Rpd3 is conserved, and eukaryotic genes frequently encode transcripts with variable 5′‐UTRs. Our findings are therefore relevant for regulatory mechanisms involved in the control of transcript isoforms in multi‐cellular organisms.</p> </abstract> … (more)
- Is Part Of:
- Molecular microbiology. Volume 96:Issue 4(2015)
- Journal:
- Molecular microbiology
- Issue:
- Volume 96:Issue 4(2015)
- Issue Display:
- Volume 96, Issue 4 (2015)
- Year:
- 2015
- Volume:
- 96
- Issue:
- 4
- Issue Sort Value:
- 2015-0096-0004-0000
- Page Start:
- 861
- Page End:
- 874
- Publication Date:
- 2015-03-21
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.12976 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3251.xml