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Histone modifying protein complexes ...
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Leader Anderson, Jennifer E.
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Histone modifying protein complexes in gene transcription.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Histone modifying protein complexes in gene transcription./
作者:
Leader Anderson, Jennifer E.
面頁冊數:
137 p.
附註:
Adviser: Richard Pestell.
Contained By:
Dissertation Abstracts International68-09B.
標題:
Biology, Cell. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3283075
ISBN:
9780549255734
Histone modifying protein complexes in gene transcription.
Leader Anderson, Jennifer E.
Histone modifying protein complexes in gene transcription.
- 137 p.
Adviser: Richard Pestell.
Thesis (Ph.D.)--Georgetown University Medical Center, 2007.
Histone modification leads to regulation of transcription through two main mechanisms, maintenance of chromatin structure and recruitment of transcriptional complexes. This study focuses on understanding how histone modifying proteins interact with non-histone proteins to regulate transcription of target genes in euchromatic regions of the genome by recruiting transcriptional complexes. I have studied the relationship between histone modifying proteins and each of the following signaling mechanisms, Bone Morphogenetic Protein (BMP) signaling, cyclin DI control of the cell cycle and PPARgamma1 expression. I demonstrate that histone modifying proteins (HMTs, HATs, HDACs and chromatin remodelers) alter target gene expression through cooperation with non-histone proteins in each example. I first examine histone methyltransferase and BMP R-Smad complexes involved in transcriptional repression in Chapter 2. Through a series of co-immunoprecipitation/Western blotting, indirect immunofluorescence and luciferase trans-activation assays, cooperation between Suv39h1, HP1 and BMP R-Smads is demonstrated. Chapter 3 focuses on interactions between the chromatin remodeling protein BRG-1, histone methyltransferases and the cell cycle regulator cyclin D1. Both BRG-1 and the HMTs are shown to regulate cyclin D1 expression through luciferase trans-activation and Chromatin Immunoprecipitation (ChIP) assays. Finally, the study of PPARgamma1 regulation by histone modifying proteins is begun in Chapter 4. PPARgamma1 acetylation is verified through cloning, acetyltransferase and luciferase trans-activation assays. Further work examines the possibility of PPARgamma1 regulation by HDAC proteins. Overall, this body of work verifies the importance of the interaction between histone modifying proteins and non-histone proteins in regulating the process of transcription.
ISBN: 9780549255734Subjects--Topical Terms:
1017686
Biology, Cell.
Histone modifying protein complexes in gene transcription.
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Histone modification leads to regulation of transcription through two main mechanisms, maintenance of chromatin structure and recruitment of transcriptional complexes. This study focuses on understanding how histone modifying proteins interact with non-histone proteins to regulate transcription of target genes in euchromatic regions of the genome by recruiting transcriptional complexes. I have studied the relationship between histone modifying proteins and each of the following signaling mechanisms, Bone Morphogenetic Protein (BMP) signaling, cyclin DI control of the cell cycle and PPARgamma1 expression. I demonstrate that histone modifying proteins (HMTs, HATs, HDACs and chromatin remodelers) alter target gene expression through cooperation with non-histone proteins in each example. I first examine histone methyltransferase and BMP R-Smad complexes involved in transcriptional repression in Chapter 2. Through a series of co-immunoprecipitation/Western blotting, indirect immunofluorescence and luciferase trans-activation assays, cooperation between Suv39h1, HP1 and BMP R-Smads is demonstrated. Chapter 3 focuses on interactions between the chromatin remodeling protein BRG-1, histone methyltransferases and the cell cycle regulator cyclin D1. Both BRG-1 and the HMTs are shown to regulate cyclin D1 expression through luciferase trans-activation and Chromatin Immunoprecipitation (ChIP) assays. Finally, the study of PPARgamma1 regulation by histone modifying proteins is begun in Chapter 4. PPARgamma1 acetylation is verified through cloning, acetyltransferase and luciferase trans-activation assays. Further work examines the possibility of PPARgamma1 regulation by HDAC proteins. Overall, this body of work verifies the importance of the interaction between histone modifying proteins and non-histone proteins in regulating the process of transcription.
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