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FtsZ Phosphorylation Modulates Tail-Core Binding to Tune Cell Division in Bacillus subtilis
FtsZ Phosphorylation Modulates Tail-Core Binding to Tune Cell Division in Bacillus subtilis
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20260202103557
- ISBN
- 9798280711723
- DDC
- 574
- 서명/저자
- FtsZ Phosphorylation Modulates Tail-Core Binding to Tune Cell Division in Bacillus subtilis
- 발행사항
- [Sl] : Harvard University, 2025
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2025
- 형태사항
- 216 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 86-12, Section: B.
- 주기사항
- Advisor: Garner, Ethan.
- 학위논문주기
- Thesis (Ph.D.)--Harvard University, 2025.
- 초록/해제
- 요약The bacterial cytoskeletal protein FtsZ orchestrates cell division in nearly all bacterial species, yet the regulatory mechanisms governing its assembly dynamics remain incompletely understood. This thesis identifies a novel intramolecular interaction within Bacillus subtilis FtsZ between its intrinsically disordered C-terminal linker (CTL) and its globular core that directly modulates FtsZ function. Through complementary biophysical, biochemical, and computational approaches, I demonstrate that the CTL specifically binds to the core's C-terminal polymerization surface with high affinity, with residues L330-H337 forming the critical binding interface. I further establish that S333 within this region is phosphorylated in a PrkC-dependent manner, suggesting post-translational regulation of this interaction.Disruption of tail-core binding through S333 mutations produces effects across multiple biological scales: at the molecular level, it reduces FtsZ's critical concentration and increases its GTPase activity; at the cellular level, it decreases cell length; and at the population level, it enhances growth under hypoxic and cell wall stress conditions in liquid culture while producing smaller colonies on solid media. Together, these findings suggest a previously uncharacterized regulatory mechanism where PrkC-mediated phosphorylation may dynamically tune FtsZ assembly, and consequently bacterial cell division, in response to environmental signals.This work reframes our understanding of FtsZ's intrinsically disordered linker from an inert mechanical tether to an active regulatory element. It further highlights how phosphorylation of disordered regions can provide functional plasticity to cytoskeletal proteins.
- 일반주제명
- Biochemistry
- 일반주제명
- Cellular biology
- 일반주제명
- Microbiology
- 일반주제명
- Molecular biology
- 키워드
- Cell division
- 기타저자
- Harvard University Biology Molecular and Cellular
- 기본자료저록
- Dissertations Abstracts International. 86-12B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
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■006m o d
■007cr#unu||||||||
■020 ▼a9798280711723
■035 ▼a(MiAaPQ)AAI32042133
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a574
■1001 ▼aMallard, William.▼0(orcid)0000-0002-2271-945X
■24510▼aFtsZ Phosphorylation Modulates Tail-Core Binding to Tune Cell Division in Bacillus subtilis
■260 ▼a[Sl]▼bHarvard University▼c2025
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2025
■300 ▼a216 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 86-12, Section: B.
■500 ▼aAdvisor: Garner, Ethan.
■5021 ▼aThesis (Ph.D.)--Harvard University, 2025.
■520 ▼aThe bacterial cytoskeletal protein FtsZ orchestrates cell division in nearly all bacterial species, yet the regulatory mechanisms governing its assembly dynamics remain incompletely understood. This thesis identifies a novel intramolecular interaction within Bacillus subtilis FtsZ between its intrinsically disordered C-terminal linker (CTL) and its globular core that directly modulates FtsZ function. Through complementary biophysical, biochemical, and computational approaches, I demonstrate that the CTL specifically binds to the core's C-terminal polymerization surface with high affinity, with residues L330-H337 forming the critical binding interface. I further establish that S333 within this region is phosphorylated in a PrkC-dependent manner, suggesting post-translational regulation of this interaction.Disruption of tail-core binding through S333 mutations produces effects across multiple biological scales: at the molecular level, it reduces FtsZ's critical concentration and increases its GTPase activity; at the cellular level, it decreases cell length; and at the population level, it enhances growth under hypoxic and cell wall stress conditions in liquid culture while producing smaller colonies on solid media. Together, these findings suggest a previously uncharacterized regulatory mechanism where PrkC-mediated phosphorylation may dynamically tune FtsZ assembly, and consequently bacterial cell division, in response to environmental signals.This work reframes our understanding of FtsZ's intrinsically disordered linker from an inert mechanical tether to an active regulatory element. It further highlights how phosphorylation of disordered regions can provide functional plasticity to cytoskeletal proteins.
■590 ▼aSchool code: 0084.
■650 4▼aBiochemistry
■650 4▼aCellular biology
■650 4▼aMicrobiology
■650 4▼aMolecular biology
■653 ▼aBacillus subtilis
■653 ▼aCell division
■653 ▼aBacterial species
■653 ▼aC-terminal linker
■690 ▼a0487
■690 ▼a0379
■690 ▼a0410
■690 ▼a0307
■71020▼aHarvard University▼bBiology, Molecular and Cellular.
■7730 ▼tDissertations Abstracts International▼g86-12B.
■790 ▼a0084
■791 ▼aPh.D.
■792 ▼a2025
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17357766▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
