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Relating Structure With Function and Mechanics of Bacterial Polymers
Relating Structure With Function and Mechanics of Bacterial Polymers
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20250211152934
- ISBN
- 9798346759447
- DDC
- 574.191
- 서명/저자
- Relating Structure With Function and Mechanics of Bacterial Polymers
- 발행사항
- [Sl] : Princeton University, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 121 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 86-06, Section: B.
- 주기사항
- Advisor: Gitai, Zemer.
- 학위논문주기
- Thesis (Ph.D.)--Princeton University, 2024.
- 초록/해제
- 요약Bacterial polymers are a diverse group of proteins involved in a wide range of functions including cell shape maintenance, subcellular localization, cell division, and plasmid segregation. These polymers are highly important to understand major cell-scale processes. The mechanical properties of bacterial polymers have been suggested to play important roles in their functions. However, there are relatively few examples available where the mechanics and structures of the same polymers are known, such that the biophysical relationships between these properties remains largely unclear. Here we study two different bacterial polymers and utilize single particle Cryo-Electron Microscopy (cryo-EM) to relate the structure of the polymers to their function and mechanics.We first studied the periplasmic copolymer CrvAB, found in Vibrio cholerae. CrvAB is comprised of two proteins CrvA and CrvB which assemble together and induce cell curvature. The curvature of V. cholerae cells improves the fitness, motility, and pathogenesis. Here we aimed to study the interactions between CrvA and CrvB and the structure of the copolymer. Using cryo-EM, we developed a 3D reconstruction of the CrvAB filaments in vitro and developed a model to fit the reconstruction. We utilized in vitro and in vivo techniques to validate the model and discovered key amino acid interactions necessary for proper functioning of the CrvAB copolymer. Excitingly, the CrvAB filaments have a unique hexagonal structure not seen in other bacterial polymers.The second bacterial polymers studied here are Type IV Pili (T4P). These bacterial polymers extend beyond the cell surface and are involved in a wide range of functions including DNA uptake, twitching motility, and virulence. We found that T4P have distinct mechanics by measuring the persistence lengths of the polymers. The sequence of the pilin subunits does not predict the measured mechanics. We instead hypothesized that the structure of the pilus filaments would dictate the mechanics of the fiber. To determine this, we prepared two distinct T4P samples and utilized cryo-EM to determine the structure of the filaments. We found that the pili that had tighter packing of monomers was less flexible compared to the more loosely packed pilus.
- 일반주제명
- Biophysics
- 일반주제명
- Microbiology
- 키워드
- Cryo-EM
- 기타저자
- Princeton University Quantitative Computational Biology
- 기본자료저록
- Dissertations Abstracts International. 86-06B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■020 ▼a9798346759447
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■040 ▼aMiAaPQ▼cMiAaPQ
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■1001 ▼aChase, Katelyn Joy.▼0(orcid)0000-0002-2715-382X
■24510▼aRelating Structure With Function and Mechanics of Bacterial Polymers
■260 ▼a[Sl]▼bPrinceton University▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a121 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 86-06, Section: B.
■500 ▼aAdvisor: Gitai, Zemer.
■5021 ▼aThesis (Ph.D.)--Princeton University, 2024.
■520 ▼aBacterial polymers are a diverse group of proteins involved in a wide range of functions including cell shape maintenance, subcellular localization, cell division, and plasmid segregation. These polymers are highly important to understand major cell-scale processes. The mechanical properties of bacterial polymers have been suggested to play important roles in their functions. However, there are relatively few examples available where the mechanics and structures of the same polymers are known, such that the biophysical relationships between these properties remains largely unclear. Here we study two different bacterial polymers and utilize single particle Cryo-Electron Microscopy (cryo-EM) to relate the structure of the polymers to their function and mechanics.We first studied the periplasmic copolymer CrvAB, found in Vibrio cholerae. CrvAB is comprised of two proteins CrvA and CrvB which assemble together and induce cell curvature. The curvature of V. cholerae cells improves the fitness, motility, and pathogenesis. Here we aimed to study the interactions between CrvA and CrvB and the structure of the copolymer. Using cryo-EM, we developed a 3D reconstruction of the CrvAB filaments in vitro and developed a model to fit the reconstruction. We utilized in vitro and in vivo techniques to validate the model and discovered key amino acid interactions necessary for proper functioning of the CrvAB copolymer. Excitingly, the CrvAB filaments have a unique hexagonal structure not seen in other bacterial polymers.The second bacterial polymers studied here are Type IV Pili (T4P). These bacterial polymers extend beyond the cell surface and are involved in a wide range of functions including DNA uptake, twitching motility, and virulence. We found that T4P have distinct mechanics by measuring the persistence lengths of the polymers. The sequence of the pilin subunits does not predict the measured mechanics. We instead hypothesized that the structure of the pilus filaments would dictate the mechanics of the fiber. To determine this, we prepared two distinct T4P samples and utilized cryo-EM to determine the structure of the filaments. We found that the pili that had tighter packing of monomers was less flexible compared to the more loosely packed pilus.
■590 ▼aSchool code: 0181.
■650 4▼aBiophysics
■650 4▼aMicrobiology
■653 ▼aBacterial polymers
■653 ▼aCryo-EM
■653 ▼aStructural biology
■690 ▼a0786
■690 ▼a0410
■71020▼aPrinceton University▼bQuantitative Computational Biology.
■7730 ▼tDissertations Abstracts International▼g86-06B.
■790 ▼a0181
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17164210▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
