Language:
English
繁體中文
Help
回圖書館首頁
手機版館藏查詢
Login
Back
Switch To:
Labeled
|
MARC Mode
|
ISBD
Histone modifying protein complexes ...
~
Leader Anderson, Jennifer E.
Linked to FindBook
Google Book
Amazon
博客來
Histone modifying protein complexes in gene transcription.
Record Type:
Language materials, printed : Monograph/item
Title/Author:
Histone modifying protein complexes in gene transcription./
Author:
Leader Anderson, Jennifer E.
Description:
137 p.
Notes:
Adviser: Richard Pestell.
Contained By:
Dissertation Abstracts International68-09B.
Subject:
Biology, Cell. -
Online resource:
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.
LDR
:02770nam 2200289 a 45
001
956485
005
20110624
008
110624s2007 ||||||||||||||||| ||eng d
020
$a
9780549255734
035
$a
(UMI)AAI3283075
035
$a
AAI3283075
040
$a
UMI
$c
UMI
100
1
$a
Leader Anderson, Jennifer E.
$3
1279951
245
1 0
$a
Histone modifying protein complexes in gene transcription.
300
$a
137 p.
500
$a
Adviser: Richard Pestell.
500
$a
Source: Dissertation Abstracts International, Volume: 68-09, Section: B, page: 5876.
502
$a
Thesis (Ph.D.)--Georgetown University Medical Center, 2007.
520
$a
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.
590
$a
School code: 0544.
650
4
$a
Biology, Cell.
$3
1017686
650
4
$a
Biology, Molecular.
$3
1017719
650
4
$a
Health Sciences, Oncology.
$3
1018566
690
$a
0307
690
$a
0379
690
$a
0992
710
2
$a
Georgetown University Medical Center.
$3
1021821
773
0
$t
Dissertation Abstracts International
$g
68-09B.
790
$a
0544
790
1 0
$a
Pestell, Richard,
$e
advisor
791
$a
Ph.D.
792
$a
2007
856
4 0
$u
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3283075
based on 0 review(s)
Location:
ALL
電子資源
Year:
Volume Number:
Items
1 records • Pages 1 •
1
Inventory Number
Location Name
Item Class
Material type
Call number
Usage Class
Loan Status
No. of reservations
Opac note
Attachments
W9120714
電子資源
11.線上閱覽_V
電子書
EB W9120714
一般使用(Normal)
On shelf
0
1 records • Pages 1 •
1
Multimedia
Reviews
Add a review
and share your thoughts with other readers
Export
pickup library
Processing
...
Change password
Login