The interaction between the histone acetyltransferase complex Hat1‐Hat2 and transcription factor AmyR provides a molecular brake to regulate amylase gene expression. Issue 4 (14th February 2023)
- Record Type:
- Journal Article
- Title:
- The interaction between the histone acetyltransferase complex Hat1‐Hat2 and transcription factor AmyR provides a molecular brake to regulate amylase gene expression. Issue 4 (14th February 2023)
- Main Title:
- The interaction between the histone acetyltransferase complex Hat1‐Hat2 and transcription factor AmyR provides a molecular brake to regulate amylase gene expression
- Authors:
- Hu, Yueyan
Liu, Zhongjiao
Xu, Shaohua
Zhao, Qinqin
Liu, Guodong
Song, Xin
Qu, Yinbo
Qin, Yuqi - Abstract:
- Abstract: The chromatin structure is generally regulated by chromatin remodelers and histone modifiers, which affect DNA replication, repair, and levels of transcription. The first identified histone acetyltransferase was Hat1/KAT1, which belongs to lysine (K) acetyltransferases. The catalytic subunit Hat1 and the regulatory subunit Hat2 make up the core HAT1 complex. In this study, the results of tandem affinity purification and mass spectrometry and bimolecular fluorescence complementation proved that the Penicillium oxalicum PoHat1‐Hat2 is the transcriptional cofactor of the sequence‐specific transcription factor PoAmyR, a transcription activator essential for the transcription of amylase gene. ChIP‐qPCR results demonstrated that the complex PoHat1‐Hat2 is recruited by PoAmyR to the promoters of prominent amylase genes Po amy13A and Po amy15A and performs histone H4 lysine12 acetylation. The result of the yeast two‐hybrid test indicated that PoHat2 is the subunit that directly interacts with PoAmyR. PoHat1‐Hat2 acts as the molecular brake of the PoAmyR‐regulating transcription of amylase genes. A putative model for amylase gene regulation by PoAmyR‐Hat2‐Hat1 was constructed. Our paper is the first report that the Hat1‐Hat2 complex acts as a cofactor for sequence‐specific TF to regulate gene expression and explains the mechanism of TF AmyR regulating amylase genes expression. Abstract : Penicillium oxalicum AmyR (PoAmyR), a transcription activator essential for theAbstract: The chromatin structure is generally regulated by chromatin remodelers and histone modifiers, which affect DNA replication, repair, and levels of transcription. The first identified histone acetyltransferase was Hat1/KAT1, which belongs to lysine (K) acetyltransferases. The catalytic subunit Hat1 and the regulatory subunit Hat2 make up the core HAT1 complex. In this study, the results of tandem affinity purification and mass spectrometry and bimolecular fluorescence complementation proved that the Penicillium oxalicum PoHat1‐Hat2 is the transcriptional cofactor of the sequence‐specific transcription factor PoAmyR, a transcription activator essential for the transcription of amylase gene. ChIP‐qPCR results demonstrated that the complex PoHat1‐Hat2 is recruited by PoAmyR to the promoters of prominent amylase genes Po amy13A and Po amy15A and performs histone H4 lysine12 acetylation. The result of the yeast two‐hybrid test indicated that PoHat2 is the subunit that directly interacts with PoAmyR. PoHat1‐Hat2 acts as the molecular brake of the PoAmyR‐regulating transcription of amylase genes. A putative model for amylase gene regulation by PoAmyR‐Hat2‐Hat1 was constructed. Our paper is the first report that the Hat1‐Hat2 complex acts as a cofactor for sequence‐specific TF to regulate gene expression and explains the mechanism of TF AmyR regulating amylase genes expression. Abstract : Penicillium oxalicum AmyR (PoAmyR), a transcription activator essential for the transcription of amylase gene, recruits histone acetyltransferase complex PoHat1‐Hat2 as transcriptional cofactor via direct interaction with PoHat2 subunit. PoHat1‐Hat2 complex acts as the molecular brake of the PoAmyR‐regulating transcription of amylase genes. This is the first report that the Hat1‐Hat2 complex acts as a cofactor for sequence‐specific transcription factor to regulate transcription. … (more)
- Is Part Of:
- Molecular microbiology. Volume 119:Issue 4(2023)
- Journal:
- Molecular microbiology
- Issue:
- Volume 119:Issue 4(2023)
- Issue Display:
- Volume 119, Issue 4 (2023)
- Year:
- 2023
- Volume:
- 119
- Issue:
- 4
- Issue Sort Value:
- 2023-0119-0004-0000
- Page Start:
- 471
- Page End:
- 491
- Publication Date:
- 2023-02-14
- Subjects:
- amylase -- cofactors -- fungi -- histone acetyltransferases -- transcription factors
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.15036 ↗
- 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:
- 26964.xml