DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | Seo, Yeon-Soo | - |
dc.contributor.advisor | 서연수 | - |
dc.contributor.author | Phung Thi Thu, Huong | - |
dc.date.accessioned | 2017-03-29T02:44:46Z | - |
dc.date.available | 2017-03-29T02:44:46Z | - |
dc.date.issued | 2015 | - |
dc.identifier.uri | http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=657554&flag=dissertation | en_US |
dc.identifier.uri | http://hdl.handle.net/10203/222108 | - |
dc.description | 학위논문(박사) - 한국과학기술원 : 생명과학과, 2015.2 ,[vii, 100 p. :] | - |
dc.description.abstract | Mus81-Mms4 and Fen1 are DNA endonucleases involved in processing of a variety of DNA structural intermediates formed during DNA transactions such as replication and ho-mologous recombination. Recently, it was reported that Mus81 physically interacts with Rad27 (yeast Fen1) and they are mutually stimulatory in a manner dependent on specific pro-tein-protein interactions. In this paper, we investigated the in vivo significance of the interac-tions observed between the two enzymes and showed that the N-terminal 120 amino-acid re-gion of Mus81 was required for functional interactions with Rad27. Mus81 $\Delta$ 120N lacking the N-terminal 120 amino-acid region displayed catalytic activity comparable to that wild-type when it formed a complex with Mms4, but failed to be stimulated by Rad27. Interestingly, the mus81 $\Delta$ 120N allele showed synthetic lethality when combined with sgs1$\Delta$. Considering that Sgs1 constitutes an alternative pathway in parallel to Mus81-Mms4, our results suggest that the physical and functional interactions observed between Mus81 and Rad27 are physiologically important in resolving toxic recombination intermediates. In support of this, the lethality of sgs1$\Delta$ mus81 $\Delta$ 120N was efficiently rescued by further deletion of RAD52, a key recombination mediator essential to generate the toxic intermediates. Mutagenic analyses of the N-terminal region identified two distinct motifs, named N21-26 (aa from 21-26) and N108-114 (aa from 108-114) important for the in vitro and in vivo functions of Mus81. Our findings indicate that the N-terminal region of Mus81 acts as a landing pad to interact with Rad27 and that Mus81 and Rad27 work conjointly for efficient removal of various aberrant DNA structures. | - |
dc.language | eng | - |
dc.publisher | 한국과학기술원 | - |
dc.subject | Mus81 | - |
dc.subject | Fen1 | - |
dc.subject | Sgs1 | - |
dc.subject | protein-protein interaction | - |
dc.subject | homologous recombination repair | - |
dc.subject | 단백질 - 단백질 상호 작용 | - |
dc.subject | 상동 재조합 수리 | - |
dc.title | (A) physiological significance of the functional interaction between mus81 and fen1 in homologous recombination repair | - |
dc.title.alternative | 상동 재조합에 있어 Mus81과 Fen1의 기능적 상호작용이 가지는 생물학적 중요성 | - |
dc.type | Thesis(Ph.D) | - |
dc.identifier.CNRN | 325007 | - |
dc.description.department | 한국과학기술원 :생명과학과, | - |
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