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Elucidating How the Gamma-Tubulin Ring Complex (γ-TuRC) Nucleates Microtubules- [electronic resource]
Elucidating How the Gamma-Tubulin Ring Complex (γ-TuRC) Nucleates Microtubules- [electronic resource]
상세정보
- 자료유형
- 학위논문파일 국외
- 최종처리일시
- 20240214100116
- ISBN
- 9798379720520
- DDC
- 574
- 서명/저자
- Elucidating How the Gamma-Tubulin Ring Complex (γ-TuRC) Nucleates Microtubules - [electronic resource]
- 발행사항
- [S.l.]: : Princeton University., 2023
- 발행사항
- Ann Arbor : : ProQuest Dissertations & Theses,, 2023
- 형태사항
- 1 online resource(110 p.)
- 주기사항
- Source: Dissertations Abstracts International, Volume: 84-12, Section: B.
- 주기사항
- Advisor: Petry, Sabine.
- 학위논문주기
- Thesis (Ph.D.)--Princeton University, 2023.
- 사용제한주기
- This item must not be sold to any third party vendors.
- 초록/해제
- 요약Microtubules (MTs) are dynamic cylindrical polymers made of α/β-tubulin dimers that function in many diverse and essential cellular processes such as cell division, intracellular transport, and organelle positioning. Because of their importance, it is imperative that microtubules are nucleated at the correct time and place. A protein known to be essential for MT nucleation is γ-tubulin, which together with other proteins in the cell, forms a ring-like template called the γ-tubulin ring complex (γ-TuRC). Despite its importance, little is known about how the γ-TuRC nucleates MTs. For many years, it has been proposed that the γ-TuRC undergoes a large structural change upon activation, though this has not been observed directly. In this dissertation, I present two complementary structures of the γ-TuRC. The first structure is a cryo-electron microscopy (cryo-EM) structure of the γ-TuRC with an activating protein domain, which shows dynamic movement within the complex. While theorized for many years, I present the first example of structural changes that occur to change the diameter of the γ-TuRC. The second structure is the first cryo-electron tomography (cryo-ET) sub-tomogram average of the γ-TuRC in a post-nucleation state. This reconstruction of the γ-TuRC bound to a MT provides insight into the position of the γ-TuRC in relation to a newly formed MT. Together, my work helps to further our understanding of how the universal MT nucleator, the γ-TuRC, functions to regulate the production of MTs.
- 일반주제명
- Molecular biology.
- 일반주제명
- Biochemistry.
- 일반주제명
- Cellular biology.
- 키워드
- Microtubule
- 기타저자
- Princeton University Molecular Biology
- 기본자료저록
- Dissertations Abstracts International. 84-12B.
- 기본자료저록
- Dissertation Abstract International
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■00520240214100116
■006m o d
■007cr#unu||||||||
■020 ▼a9798379720520
■035 ▼a(MiAaPQ)AAI30422839
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a574
■1001 ▼aRomer, Brianna Lynne.
■24510▼aElucidating How the Gamma-Tubulin Ring Complex (γ-TuRC) Nucleates Microtubules▼h[electronic resource]
■260 ▼a[S.l.]:▼bPrinceton University. ▼c2023
■260 1▼aAnn Arbor :▼bProQuest Dissertations & Theses, ▼c2023
■300 ▼a1 online resource(110 p.)
■500 ▼aSource: Dissertations Abstracts International, Volume: 84-12, Section: B.
■500 ▼aAdvisor: Petry, Sabine.
■5021 ▼aThesis (Ph.D.)--Princeton University, 2023.
■506 ▼aThis item must not be sold to any third party vendors.
■520 ▼aMicrotubules (MTs) are dynamic cylindrical polymers made of α/β-tubulin dimers that function in many diverse and essential cellular processes such as cell division, intracellular transport, and organelle positioning. Because of their importance, it is imperative that microtubules are nucleated at the correct time and place. A protein known to be essential for MT nucleation is γ-tubulin, which together with other proteins in the cell, forms a ring-like template called the γ-tubulin ring complex (γ-TuRC). Despite its importance, little is known about how the γ-TuRC nucleates MTs. For many years, it has been proposed that the γ-TuRC undergoes a large structural change upon activation, though this has not been observed directly. In this dissertation, I present two complementary structures of the γ-TuRC. The first structure is a cryo-electron microscopy (cryo-EM) structure of the γ-TuRC with an activating protein domain, which shows dynamic movement within the complex. While theorized for many years, I present the first example of structural changes that occur to change the diameter of the γ-TuRC. The second structure is the first cryo-electron tomography (cryo-ET) sub-tomogram average of the γ-TuRC in a post-nucleation state. This reconstruction of the γ-TuRC bound to a MT provides insight into the position of the γ-TuRC in relation to a newly formed MT. Together, my work helps to further our understanding of how the universal MT nucleator, the γ-TuRC, functions to regulate the production of MTs.
■590 ▼aSchool code: 0181.
■650 4▼aMolecular biology.
■650 4▼aBiochemistry.
■650 4▼aCellular biology.
■653 ▼aCryo-electron microscopy
■653 ▼aCryo-electron tomography
■653 ▼aGamma-tubulin ring complex
■653 ▼aMicrotubule
■653 ▼aCylindrical polymers
■690 ▼a0307
■690 ▼a0487
■690 ▼a0379
■71020▼aPrinceton University▼bMolecular Biology.
■7730 ▼tDissertations Abstracts International▼g84-12B.
■773 ▼tDissertation Abstract International
■790 ▼a0181
■791 ▼aPh.D.
■792 ▼a2023
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T16931778▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
■980 ▼a202402▼f2024
