Study on the three-dimensional reconstruction of APOBEC3G–Vif–CBF\beta–ElonginB–ElonginC–Cullin5 complex = APOBEC3G–Vif–CBF\beta–ElonginB–ElonginC–Cullin5 컴플렉스의 3차원 구조 재구축에 관한 연구

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Human APOBEC3G (A3G) is an innate immunity protein against human immunodeficient virus (HIV) by deaminating cytosine into uracil on reverse transcripted single-stranded DNA of HIV. Vif, a HIV protein that functions as a substrate receptor together with Elongin BC complex and CBF\beta, for the Cullin 5-based E3 ligase complex, leads to ubiquitination and subsequent proteosomal degradation of A3G. To date, the structural information of this A3G-Vif bound E3 ligase complex is limited, as the structure of full-length A3G is not revealed since its self-oligomerizing nature of A3G. Here, we report three dimensional reconsturction of the hexameric complex of full-length A3G and Vif–CBF\beta–Elongin B–Elongin C–Cullin5 by using negative staining electron microscopy and chemical crosslinking. YFP tagged on N-terminal domain of A3G revealed that A3G dimerizes through its N-terminal domain, also A3G and Vif–CBF\beta– ElonginB–ElonginC–Cullin5 is forming 2:1 complex. Chemical crosslinking of lysines, followed by mass spectrometry also provides an evidence of N-terminal dimerization of A3G, while having a novel hydrophobic interface consisted of helix α6 to helix α6’. Full-model construction of E3 ligase, A3G–Vif–CBF\beta–Elongin B–Elongin C–Cul5–Rbx1–UbcH5–ubiquitin, providing structural basis of Vif-mediated A3G ubiquitination mechanism.
Advisors
Oh, Byung-Haresearcher오병하researcher
Description
한국과학기술원 :생명과학과,
Publisher
한국과학기술원
Issue Date
2018
Identifier
325007
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생명과학과, 2018.8,[ii, 41 p. :]

Keywords

HIV-1 Vif▼aAPOBEC3G▼aCullin5 E3 ligase complex▼aEM 3D reconstruction▼aA3G

URI
http://hdl.handle.net/10203/266277
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=828508&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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