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Recognition of Histone 3 Lysine 9 Dimethylation Regulates Its Production
Recognition of Histone 3 Lysine 9 Dimethylation Regulates Its Production
Detailed Information
- Material Type
- 단행본
- 0017160380
- Date and Time of Latest Transaction
- 20250211151008
- ISBN
- 9798381972153
- DDC
- 574
- Author
- Simental, Eric.
- Title/Author
- Recognition of Histone 3 Lysine 9 Dimethylation Regulates Its Production
- Publish Info
- [Sl] : University of California, San Francisco, 2024
- Publish Info
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- Material Info
- 82 p
- General Note
- Source: Dissertations Abstracts International, Volume: 85-09, Section: B.
- General Note
- Advisor: Cool, Abigail.
- 학위논문주기
- Thesis (Ph.D.)--University of California, San Francisco, 2024.
- Abstracts/Etc
- 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.
- Subject Added Entry-Topical Term
- Molecular biology
- Subject Added Entry-Topical Term
- Biochemistry
- Index Term-Uncontrolled
- Cell Identity Regulation
- Index Term-Uncontrolled
- Chromatin Dynamics
- Index Term-Uncontrolled
- G9a-GLP Heterodimer
- Index Term-Uncontrolled
- Histone 3 Lysine 9 Dimethylation (H3K9me2)
- Index Term-Uncontrolled
- Nucleosome Methylation
- Index Term-Uncontrolled
- Protein-Protein Interactions
- Added Entry-Corporate Name
- University of California, San Francisco Biochemistry and Molecular Biology
- Host Item Entry
- Dissertations Abstracts International. 85-09B.
- Electronic Location and Access
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■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.
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