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The Histone Chaperone Spt6 Controls Chromatin Structure Through Its Conserved N-Terminal Domain
The Histone Chaperone Spt6 Controls Chromatin Structure Through Its Conserved N-Terminal Domain
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20260202103541
- ISBN
- 9798280709966
- DDC
- 575
- 저자명
- Warner, James L.
- 서명/저자
- The Histone Chaperone Spt6 Controls Chromatin Structure Through Its Conserved N-Terminal Domain
- 발행사항
- [Sl] : Harvard University, 2025
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2025
- 형태사항
- 161 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 86-12, Section: B.
- 주기사항
- Advisor: Winston, Fred.
- 학위논문주기
- Thesis (Ph.D.)--Harvard University, 2025.
- 초록/해제
- 요약The disassembly and reassembly of nucleosomes by histone chaperones is an essential activity during eukaryotic transcription elongation. This highly conserved process maintains chromatin integrity by transiently removing nucleosomes as barriers and then restoring them in the wake of transcription. While transcription elongation requires multiple histone chaperones, there is little understanding of how most of them function and why so many are required. Here, we show that the histone chaperone Spt6 acts through its acidic, intrinsically disordered N-terminal domain (NTD) to bind histones and control chromatin structure. The Spt6 NTD is essential for viability and its histone binding activity is conserved between yeast and humans. The essential nature of the Spt6 NTD can be bypassed by changes in another histone chaperone, FACT, revealing a close functional connection between the two. Our results have led to a mechanistic model for dynamic cooperation between multiple histone chaperones during transcription elongation.
- 일반주제명
- Genetics
- 일반주제명
- Biology
- 일반주제명
- Molecular biology
- 일반주제명
- Cellular biology
- 키워드
- Chromatin
- 키워드
- Nucleosome
- 기타저자
- Harvard University Biological and Biomedical Sciences
- 기본자료저록
- Dissertations Abstracts International. 86-12B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■020 ▼a9798280709966
■035 ▼a(MiAaPQ)AAI32040893
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a575
■1001 ▼aWarner, James L.▼0(orcid)0000-0002-7960-7360
■24510▼aThe Histone Chaperone Spt6 Controls Chromatin Structure Through Its Conserved N-Terminal Domain
■260 ▼a[Sl]▼bHarvard University▼c2025
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2025
■300 ▼a161 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 86-12, Section: B.
■500 ▼aAdvisor: Winston, Fred.
■5021 ▼aThesis (Ph.D.)--Harvard University, 2025.
■520 ▼aThe disassembly and reassembly of nucleosomes by histone chaperones is an essential activity during eukaryotic transcription elongation. This highly conserved process maintains chromatin integrity by transiently removing nucleosomes as barriers and then restoring them in the wake of transcription. While transcription elongation requires multiple histone chaperones, there is little understanding of how most of them function and why so many are required. Here, we show that the histone chaperone Spt6 acts through its acidic, intrinsically disordered N-terminal domain (NTD) to bind histones and control chromatin structure. The Spt6 NTD is essential for viability and its histone binding activity is conserved between yeast and humans. The essential nature of the Spt6 NTD can be bypassed by changes in another histone chaperone, FACT, revealing a close functional connection between the two. Our results have led to a mechanistic model for dynamic cooperation between multiple histone chaperones during transcription elongation.
■590 ▼aSchool code: 0084.
■650 4▼aGenetics
■650 4▼aBiology
■650 4▼aMolecular biology
■650 4▼aCellular biology
■653 ▼aChromatin
■653 ▼aHistone chaperone
■653 ▼aNucleosome
■653 ▼aTranscription elongation
■653 ▼aN-terminal domain
■690 ▼a0369
■690 ▼a0306
■690 ▼a0307
■690 ▼a0379
■71020▼aHarvard University▼bBiological and Biomedical Sciences.
■7730 ▼tDissertations Abstracts International▼g86-12B.
■790 ▼a0084
■791 ▼aPh.D.
■792 ▼a2025
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17357645▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
