Structural peculiarities of the (MHF1-MHF2)(4) octamer provide a long DNA binding patch to anchor the MHF-FANCM complex to chromatin: A solution SAXS study
文献类型：期刊论文
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| 作者 | Wang WJ(王文佳) ; Wang, WJ; Guo, Q; Shtykova, EV; Liu, GF; Xu, JH; Teng, MK; Liu, P; Dong, YH;; Liu GF(刘广峰)
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| 刊名 | FEBS LETTERS
 ; FEBS LETTERS
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| 出版日期 | 2013 ; 2013 |
| 卷号 | 587期号:18页码:2912-2917 |
| 关键词 | Fanconi anaemia MHF complex FANCM DNA binding patch SAXS Fanconi anaemia MHF complex FANCM DNA binding patch SAXS |
| ISSN号 | 0014-5793 |
| DOI | 10.1016/j.febslet.2013.07.022 |
| 英文摘要 | MHF1 and MHF2 are histone-fold-containing FANCM-associated proteins. FANCM is a Fanconi anemia (FA) complementation group protein. We previously obtained high-resolution structures of MHF1-MHF2 (MHF) and MHF in complex with a fragment of FANCM (MHF-FANCM-F). Here, we use small angle X-ray scattering (SAXS) to investigate the solution behaviors of these protein complexes. In combination with crystallographic data, the results of the SAXS study reveal that a long, positively charged patch exposed on the surface of the MHF complex plays a critical role in double-stranded DNA (dsDNA) binding. Structured summary of protein interactions: MHF2, MHF1 and FANCM-F physically interact by molecular sieving (View interaction) MHF1 and MHF2 bind by X ray scattering (View interaction) MHF1 and MHF2 bind by molecular sieving (View interaction) MHF1, FANCM-F and MHF2 physically interact by X ray scattering (View interaction) (C) 2013 Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.; MHF1 and MHF2 are histone-fold-containing FANCM-associated proteins. FANCM is a Fanconi anemia (FA) complementation group protein. We previously obtained high-resolution structures of MHF1-MHF2 (MHF) and MHF in complex with a fragment of FANCM (MHF-FANCM-F). Here, we use small angle X-ray scattering (SAXS) to investigate the solution behaviors of these protein complexes. In combination with crystallographic data, the results of the SAXS study reveal that a long, positively charged patch exposed on the surface of the MHF complex plays a critical role in double-stranded DNA (dsDNA) binding. Structured summary of protein interactions: MHF2, MHF1 and FANCM-F physically interact by molecular sieving (View interaction) MHF1 and MHF2 bind by X ray scattering (View interaction) MHF1 and MHF2 bind by molecular sieving (View interaction) MHF1, FANCM-F and MHF2 physically interact by X ray scattering (View interaction) (C) 2013 Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics; Cell Biology ; Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000324033700003 ; WOS:000324033700003 |
| 公开日期 | 2016-05-03 |
| 源URL | [http://ir.ihep.ac.cn/handle/311005/224217]  |
| 专题 | 中国科学院高能物理研究所 |
| 推荐引用方式 GB/T 7714 | Wang WJ,Wang, WJ,Guo, Q,et al. Structural peculiarities of the (MHF1-MHF2)(4) octamer provide a long DNA binding patch to anchor the MHF-FANCM complex to chromatin: A solution SAXS study, Structural peculiarities of the (MHF1-MHF2)(4) octamer provide a long DNA binding patch to anchor the MHF-FANCM complex to chromatin: A solution SAXS study[J]. FEBS LETTERS, FEBS LETTERS,2013, 2013,587, 587(18):2912-2917, 2912-2917. |
| APA | 王文佳.,Wang, WJ.,Guo, Q.,Shtykova, EV.,Liu, GF.,...&董宇辉.(2013).Structural peculiarities of the (MHF1-MHF2)(4) octamer provide a long DNA binding patch to anchor the MHF-FANCM complex to chromatin: A solution SAXS study.FEBS LETTERS,587(18),2912-2917. |
| MLA | 王文佳,et al."Structural peculiarities of the (MHF1-MHF2)(4) octamer provide a long DNA binding patch to anchor the MHF-FANCM complex to chromatin: A solution SAXS study".FEBS LETTERS 587.18(2013):2912-2917. |
入库方式： OAI收割
来源：高能物理研究所
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