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Recognition of Histone 3 Lysine 9 Dimethylation Regulates Its Production
Recognition of Histone 3 Lysine 9 Dimethylation Regulates Its Production
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20250211151008
- ISBN
- 9798381972153
- DDC
- 574
- 저자명
- Simental, Eric.
- 서명/저자
- Recognition of Histone 3 Lysine 9 Dimethylation Regulates Its Production
- 발행사항
- [Sl] : University of California, San Francisco, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 82 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 85-09, Section: B.
- 주기사항
- Advisor: Cool, Abigail.
- 학위논문주기
- Thesis (Ph.D.)--University of California, San Francisco, 2024.
- 초록/해제
- 요약Specifying cellular identity requires silencing cell-type inappropriate genes. In eukaryotes, this is accomplished by varying the packaging density of nucleosomes, segmenting chromosomes into regions of tight (heterochromatin) and loose (euchromatin) packing. Packaging is directed in part by dimethylation of Histone 3 lysine 9 (H3K9me2). H3K9me2 is catalyzed by the G9a-GLP heterodimer, which, like other heterochromatic lysine methyltransferases, possess product-recognition, or 'reading' domains. We first explore how reading by G9a-GLP affects nucleosome methylation in vitro. We unveil that a cis composition of heterotypic product-recognition domains functions to regulate nucleosome dimethylation but not monomethylation. Our findings illuminate the pivotal role of methyl nucleosome binding by these domains in facilitating dimethylation. We then turn our attention to the cell, where H3K9me2 is enriched at the nuclear periphery. We find that knocking out putative H3K9me2 readers, which releases the mark from the nuclear periphery, affects the genomic abundance and distribution of H3K9me2 specifically during differentiation. These insights underscore the complexity of the methylation landscape and open doors to understanding the interplay of molecular recognition and enzymatic activity in chromatin modification and ultimately, cell identity.
- 일반주제명
- Molecular biology
- 일반주제명
- Biochemistry
- 기타저자
- University of California, San Francisco Biochemistry and Molecular Biology
- 기본자료저록
- Dissertations Abstracts International. 85-09B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■00520250211151008
■006m o d
■007cr#unu||||||||
■020 ▼a9798381972153
■035 ▼a(MiAaPQ)AAI30995036
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a574
■1001 ▼aSimental, Eric.▼0(orcid)0000-0002-8638-6578
■24510▼aRecognition of Histone 3 Lysine 9 Dimethylation Regulates Its Production
■260 ▼a[Sl]▼bUniversity of California, San Francisco▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a82 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 85-09, Section: B.
■500 ▼aAdvisor: Cool, Abigail.
■5021 ▼aThesis (Ph.D.)--University of California, San Francisco, 2024.
■520 ▼aSpecifying cellular identity requires silencing cell-type inappropriate genes. In eukaryotes, this is accomplished by varying the packaging density of nucleosomes, segmenting chromosomes into regions of tight (heterochromatin) and loose (euchromatin) packing. Packaging is directed in part by dimethylation of Histone 3 lysine 9 (H3K9me2). H3K9me2 is catalyzed by the G9a-GLP heterodimer, which, like other heterochromatic lysine methyltransferases, possess product-recognition, or 'reading' domains. We first explore how reading by G9a-GLP affects nucleosome methylation in vitro. We unveil that a cis composition of heterotypic product-recognition domains functions to regulate nucleosome dimethylation but not monomethylation. Our findings illuminate the pivotal role of methyl nucleosome binding by these domains in facilitating dimethylation. We then turn our attention to the cell, where H3K9me2 is enriched at the nuclear periphery. We find that knocking out putative H3K9me2 readers, which releases the mark from the nuclear periphery, affects the genomic abundance and distribution of H3K9me2 specifically during differentiation. These insights underscore the complexity of the methylation landscape and open doors to understanding the interplay of molecular recognition and enzymatic activity in chromatin modification and ultimately, cell identity.
■590 ▼aSchool code: 0034.
■650 4▼aMolecular biology
■650 4▼aBiochemistry
■653 ▼aCell Identity Regulation
■653 ▼aChromatin Dynamics
■653 ▼aG9a-GLP Heterodimer
■653 ▼aHistone 3 Lysine 9 Dimethylation (H3K9me2)
■653 ▼aNucleosome Methylation
■653 ▼aProtein-Protein Interactions
■690 ▼a0307
■690 ▼a0487
■71020▼aUniversity of California, San Francisco▼bBiochemistry and Molecular Biology.
■7730 ▼tDissertations Abstracts International▼g85-09B.
■790 ▼a0034
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17160380▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
