Identification and characterization of histone globular domain-binding proteins = 히스톤 글로불러 도메인과 상호작용하는 단백질 동정 및 분석

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Until now, interacting proteins of globular domain histone modification have been rarely identified because of its structural technical limitations. Recently, the amber codon suppression method has been developed to overcome the structural limitations and I will apply this method to my research. The site specifically modified nucleosome is reconstituted and pulled down with nuclear extracts. First I focused on the most famous and much studied H3K56Ac and H3K79Me. Before discovering the interaction candidate proteins, I found the effect of H3K56Ac and H3K79Me on transcription efficiency. Both histone modifications are characterized by the activation of transcription. Therefore, finding a protein that binds directly to these modifications will provide an in-depth understanding of transcription regulation mechanisms. In addition, various in vitro assays developed through this study will be the leading studies in the epigenetic study field.
Advisors
Kim, Jaehoonresearcher김재훈researcher
Description
한국과학기술원 :생명과학과,
Publisher
한국과학기술원
Issue Date
2018
Identifier
325007
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생명과학과, 2018.2,[iii, 24 p. :]

Keywords

Eukaryotic Transcription▼aEpigenetics▼aProteomics▼aH3K56Ac▼aH3K79Me; 진핵세포 전사▼a후성유전체학▼a단백질체학▼a히스톤 H3 라이신 56 아세틸화▼a히스톤 H3 라이신 79 메틸화

URI
http://hdl.handle.net/10203/266276
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=733867&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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