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Interrogation of Intermolecular Interactions in Liquid-Liquid Phase Separation
Interrogation of Intermolecular Interactions in Liquid-Liquid Phase Separation
Interrogation of Intermolecular Interactions in Liquid-Liquid Phase Separation

상세정보

자료유형  
 학위논문 서양
최종처리일시  
20260202104824
ISBN  
9798290910611
DDC  
540
저자명  
Xu, Ruiwen.
서명/저자  
Interrogation of Intermolecular Interactions in Liquid-Liquid Phase Separation
발행사항  
[Sl] : The University of Wisconsin - Madison, 2025
발행사항  
Ann Arbor : ProQuest Dissertations & Theses, 2025
형태사항  
264 p
주기사항  
Source: Dissertations Abstracts International, Volume: 87-01, Section: B.
주기사항  
Advisor: Gellman, Samuel H.
학위논문주기  
Thesis (Ph.D.)--The University of Wisconsin - Madison, 2025.
초록/해제  
요약Liquid-liquid phase separation (LLPS) plays an important role in many cellular processes. The RNA-binding protein Fused in Sarcoma (FUS) has been shown to mediate phase separation through attractive interactions between the tyrosine-rich N-terminal domain and the arginine-rich C-terminal domain. Cation-π interactions between Arg and Tyr side chains have been proposed as a driving force for condensed phase formation involving FUS and related proteins. To explore this hypothesis, we developed a two-component system comprising a long Arg-rich FUS fragment, generated via heterologous expression, and a short Tyr-rich peptide, generated via chemical synthesis. Phase separation occurs when these components are mixed at low concentrations (5 μM each). Global replacement of Tyr with noncanonical residues allowed us to interrogate the role of the phenolic side chain in driving the polypeptide assembly that underlies condensed phase formation. The results suggest that cation-π interactions do not make a major contribution to inter- peptide attractions in our model system. Instead, the H-bond donor properties of the Tyr side chain hydroxyl appear to play a central role in driving phase separation.
일반주제명  
Chemistry
일반주제명  
Cellular biology
일반주제명  
Biochemistry
일반주제명  
Genetics
키워드  
Liquid-liquid phase separation
키워드  
Fused in Sarcoma
키워드  
Cation-π interactions
키워드  
Phase separation
키워드  
Heterologous expression
기타저자  
The University of Wisconsin - Madison Chemistry
기본자료저록  
Dissertations Abstracts International. 87-01B.
전자적 위치 및 접속  
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■006m          o    d                
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■020    ▼a9798290910611
■035    ▼a(MiAaPQ)AAI32169675
■040    ▼aMiAaPQ▼cMiAaPQ
■0820  ▼a540
■1001  ▼aXu,  Ruiwen.
■24510▼aInterrogation  of  Intermolecular  Interactions  in  Liquid-Liquid  Phase  Separation
■260    ▼a[Sl]▼bThe  University  of  Wisconsin  -  Madison▼c2025
■260  1▼aAnn  Arbor▼bProQuest  Dissertations  &  Theses▼c2025
■300    ▼a264  p
■500    ▼aSource:  Dissertations  Abstracts  International,  Volume:  87-01,  Section:  B.
■500    ▼aAdvisor:  Gellman,  Samuel  H.
■5021  ▼aThesis  (Ph.D.)--The  University  of  Wisconsin  -  Madison,  2025.
■520    ▼aLiquid-liquid  phase  separation  (LLPS)  plays  an  important  role  in  many  cellular  processes.  The  RNA-binding  protein  Fused  in  Sarcoma  (FUS)  has  been  shown  to  mediate  phase  separation  through  attractive  interactions  between  the  tyrosine-rich  N-terminal  domain  and  the  arginine-rich  C-terminal  domain.  Cation-π  interactions  between  Arg  and  Tyr  side  chains  have  been  proposed  as  a  driving  force  for  condensed  phase  formation  involving  FUS  and  related  proteins.  To  explore  this  hypothesis,  we  developed  a  two-component  system  comprising  a  long  Arg-rich  FUS  fragment,  generated  via  heterologous  expression,  and  a  short  Tyr-rich  peptide,  generated  via  chemical  synthesis.  Phase  separation  occurs  when  these  components  are  mixed  at  low  concentrations  (5  μM  each).  Global  replacement  of  Tyr  with  noncanonical  residues  allowed  us  to  interrogate  the  role  of  the  phenolic  side  chain  in  driving  the  polypeptide  assembly  that  underlies  condensed  phase  formation.  The  results  suggest  that  cation-π  interactions  do  not  make  a  major  contribution  to  inter-  peptide  attractions  in  our  model  system.  Instead,  the  H-bond  donor  properties  of  the  Tyr  side  chain  hydroxyl  appear  to  play  a  central  role  in  driving  phase  separation.
■590    ▼aSchool  code:  0262.
■650  4▼aChemistry
■650  4▼aCellular  biology
■650  4▼aBiochemistry
■650  4▼aGenetics
■653    ▼aLiquid-liquid  phase  separation
■653    ▼aFused  in  Sarcoma
■653    ▼aCation-π  interactions
■653    ▼aPhase  separation
■653    ▼aHeterologous  expression
■690    ▼a0485
■690    ▼a0379
■690    ▼a0487
■690    ▼a0369
■71020▼aThe  University  of  Wisconsin  -  Madison▼bChemistry.
■7730  ▼tDissertations  Abstracts  International▼g87-01B.
■790    ▼a0262
■791    ▼aPh.D.
■792    ▼a2025
■793    ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17359032▼nKERIS▼z이  자료의  원문은  한국교육학술정보원에서  제공합니다.

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