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Approaches to Investigating Differences in MRNA Translational Machinery Across Cell Types and Subcellular Compartments
Approaches to Investigating Differences in MRNA Translational Machinery Across Cell Types and Subcellular Compartments
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20260202104739
- ISBN
- 9798290651767
- DDC
- 612
- 서명/저자
- Approaches to Investigating Differences in MRNA Translational Machinery Across Cell Types and Subcellular Compartments
- 발행사항
- [Sl] : Stanford University, 2025
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2025
- 형태사항
- 236 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 87-01, Section: B.
- 주기사항
- Includes supplementary digital materials.
- 주기사항
- Advisor: Barna, Maria.
- 학위논문주기
- Thesis (Ph.D.)--Stanford University, 2025.
- 초록/해제
- 요약The complexity of mRNA translational machinery is commensurate with the magnitude and diversity of the tasks it performs in order to safely and effectively express all protein-coding genes. This dissertation consists of two projects, each of which takes a different approach to characterizing the ribosome and other associated components of translational machinery. In Chapter 1, I provide context for these works by describing the extensive set of demands that translational machinery must fulfill, particularly in highly compartmentalized eukaryotic cells and across differentiated cell types in metazoan organisms. I also review the major known ways in which translational machinery composition varies across different biological settings, which offer a glimpse into how this machinery executes its many diverse tasks. I then examine the experimental challenges of studying translation. In Chapter 2, I explore a case study of two paralogous genes that encode similar versions of a ribosomal protein. These paralogs are conserved among vertebrates and exhibit cell type-dependent expression. To investigate why this gene duplication has been evolutionarily retained, I employ a paralog homogenization strategy by generating mouse models in which each paralog's encoded protein has been exchanged for the other. I conclude that the two paralogs encode functionally interchangeable proteins and have been evolutionarily preserved mainly through subfunctionalization of gene expression. In Chapter 3, I describe the development of a novel strategy for isolating translational machinery from subcellular compartments that is compatible with mammalian cell culture, and I present data from the initial applications of this tool towards comparing translational machinery composition and ribosome-bound mRNA between organelles. Lastly, I conclude in Chapter 4 with broader reflections on these two projects and a perspective on extending this work in the future.
- 일반주제명
- Physiology
- 일반주제명
- Cytoplasm
- 일반주제명
- Ribonucleic acid--RNA
- 일반주제명
- Biosynthesis
- 일반주제명
- Amino acids
- 일반주제명
- Mitochondria
- 일반주제명
- Genomes
- 일반주제명
- Metabolism
- 일반주제명
- Yeast
- 일반주제명
- Visualization
- 일반주제명
- Cell cycle
- 일반주제명
- Cell culture
- 일반주제명
- Protein synthesis
- 일반주제명
- Mass spectrometry
- 일반주제명
- CRISPR
- 일반주제명
- Gene expression
- 일반주제명
- Microscopy
- 일반주제명
- Alibi
- 일반주제명
- Stem cells
- 일반주제명
- Postpartum period
- 일반주제명
- Hydrogels
- 기타저자
- Stanford University.
- 기본자료저록
- Dissertations Abstracts International. 87-01B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■020 ▼a9798290651767
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■035 ▼a(MiAaPQ)Stanfordmq462pb5837
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a612
■1001 ▼aXu, Adele Francis.
■24510▼aApproaches to Investigating Differences in MRNA Translational Machinery Across Cell Types and Subcellular Compartments
■260 ▼a[Sl]▼bStanford University▼c2025
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2025
■300 ▼a236 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 87-01, Section: B.
■500 ▼aIncludes supplementary digital materials.
■500 ▼aAdvisor: Barna, Maria.
■5021 ▼aThesis (Ph.D.)--Stanford University, 2025.
■520 ▼aThe complexity of mRNA translational machinery is commensurate with the magnitude and diversity of the tasks it performs in order to safely and effectively express all protein-coding genes. This dissertation consists of two projects, each of which takes a different approach to characterizing the ribosome and other associated components of translational machinery. In Chapter 1, I provide context for these works by describing the extensive set of demands that translational machinery must fulfill, particularly in highly compartmentalized eukaryotic cells and across differentiated cell types in metazoan organisms. I also review the major known ways in which translational machinery composition varies across different biological settings, which offer a glimpse into how this machinery executes its many diverse tasks. I then examine the experimental challenges of studying translation. In Chapter 2, I explore a case study of two paralogous genes that encode similar versions of a ribosomal protein. These paralogs are conserved among vertebrates and exhibit cell type-dependent expression. To investigate why this gene duplication has been evolutionarily retained, I employ a paralog homogenization strategy by generating mouse models in which each paralog's encoded protein has been exchanged for the other. I conclude that the two paralogs encode functionally interchangeable proteins and have been evolutionarily preserved mainly through subfunctionalization of gene expression. In Chapter 3, I describe the development of a novel strategy for isolating translational machinery from subcellular compartments that is compatible with mammalian cell culture, and I present data from the initial applications of this tool towards comparing translational machinery composition and ribosome-bound mRNA between organelles. Lastly, I conclude in Chapter 4 with broader reflections on these two projects and a perspective on extending this work in the future.
■590 ▼aSchool code: 0212.
■650 4▼aPhysiology
■650 4▼aCytoplasm
■650 4▼aRibonucleic acid--RNA
■650 4▼aBiosynthesis
■650 4▼aAmino acids
■650 4▼aMitochondria
■650 4▼aGenomes
■650 4▼aMetabolism
■650 4▼aYeast
■650 4▼aVisualization
■650 4▼aCell cycle
■650 4▼aCell culture
■650 4▼aProtein synthesis
■650 4▼aMass spectrometry
■650 4▼aCRISPR
■650 4▼aGene expression
■650 4▼aMicroscopy
■650 4▼aAlibi
■650 4▼aStem cells
■650 4▼aPostpartum period
■650 4▼aHydrogels
■690 ▼a0719
■71020▼aStanford University.
■7730 ▼tDissertations Abstracts International▼g87-01B.
■790 ▼a0212
■791 ▼aPh.D.
■792 ▼a2025
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17358702▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.


