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Mechanism of Protein Acetylation in Mitochondria

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개인저자Baeza, Josue.
단체저자명The University of Wisconsin - Madison. Biomolecular Chemistry.
서명/저자사항Mechanism of Protein Acetylation in Mitochondria.
발행사항[S.l.] : The University of Wisconsin - Madison., 2017
발행사항Ann Arbor : ProQuest Dissertations & Theses, 2017
형태사항206 p.
소장본 주기School code: 0262.
ISBN9780438024113
일반주기 Source: Dissertation Abstracts International, Volume: 79-10(E), Section: B.
Adviser: John M. Denu.
요약Reversible N-epsilon-acetylation has emerged as a widespread and regulatory modification throughout the cell. First identified on N-terminal histone tails over 50 years ago, acetylation has now been identified on over 36,000 lysine sites on orga
요약In mitochondria, acetylation generally acts as an inhibitory modification, altering protein interactions, lowered enzymatic activity and mislocalization of mitochondrial proteins. In this case, acetylation acts as a rheostat, modulating the degr
요약The mechanism of mitochondrial protein acetylation remains unknown. While there is a wealth of data supporting a dynamic and regulatory role for acetylation within mitochondria, there is very little evidence for an enzyme-catalyzed reaction. How
요약Throughout my thesis research, I have utilized chemical, biochemical, proteomic, and cellular studies to characterize protein acetylation. Specifically, I developed a mass spectrometry based approach to directly quantify lysine acetylation stoic
요약Chapter 1 introduces lysine acetylation, the various processes controlling cellular levels including enzymatic and nonenzymatic, and why quantifying acetylation stoichiometry is needed. Chapter 2 discusses the mass spectrometry based method used
일반주제명Biochemistry.
언어영어
기본자료 저록Dissertation Abstracts International79-10B(E).
Dissertation Abstract International
대출바로가기http://www.riss.kr/pdu/ddodLink.do?id=T14996556

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