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Analysis of activated structure of phosphorylated XRCC4 by small angle X-ray scattering

https://repo.qst.go.jp/records/77961
https://repo.qst.go.jp/records/77961
984ee2ef-b4ac-46a9-a947-167386678075
Item type 会議発表用資料 / Presentation(1)
公開日 2019-11-29
タイトル
タイトル Analysis of activated structure of phosphorylated XRCC4 by small angle X-ray scattering
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_c94f
資源タイプ conference object
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 Hasegawa, Maho

× Hasegawa, Maho

WEKO 860086

Hasegawa, Maho

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Nishikubo, Kai

× Nishikubo, Kai

WEKO 860087

Nishikubo, Kai

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Fujiwara, Satoru

× Fujiwara, Satoru

WEKO 860088

Fujiwara, Satoru

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Matsuo, Tatsuhito

× Matsuo, Tatsuhito

WEKO 860089

Matsuo, Tatsuhito

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Yokoya, Akinari

× Yokoya, Akinari

WEKO 860090

Yokoya, Akinari

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Hasegawa, Maho

× Hasegawa, Maho

WEKO 860091

en Hasegawa, Maho

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Nishikubo, Kai

× Nishikubo, Kai

WEKO 860092

en Nishikubo, Kai

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Fujiwara, Satoru

× Fujiwara, Satoru

WEKO 860093

en Fujiwara, Satoru

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Matsuo, Tatsuhito

× Matsuo, Tatsuhito

WEKO 860094

en Matsuo, Tatsuhito

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Yokoya, Akinari

× Yokoya, Akinari

WEKO 860095

en Yokoya, Akinari

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内容記述タイプ Abstract
内容記述 Radiation-induced double strand break (DSB) has been known to be effeciently repaired by non-homologous end joining (NHEJ). XRCC4 is involved in this pathway as a dimer in vivo. Phosphorylated XRCC4 functions as scaffold when LigIV rejoins the DSB termini. XRCC4 might form a filamentary complex with another protein, XRCC4-like factor (XLF) [1]. The structural change of XRCC4 induced by phosphorylation may play an important role to form this higher order structure. So far, using circular dichroism (CD) method, we clarified the secondary structure of XRCC4 wild type and variant in which the serine-320 was substituted to an aspartic acid (denoted as S320D) to mimic phosphorylation. There is no significant difference of the XRCC4 dimer structures between the wild and S320D [2]. On the other hand, for the multimer, the secondary structure was different between the two proteins. In this study, we further worked on small angle X-ray scattering (SAXS) analysis and dynamic light scattering (DLS) to obtain conformational aspects. Although the obtained SAXS curve of variant was different from that of wild type, the dimer sample might contain certain amount of multimers. We have to estimate the effect of multimers in the curves, as well as improve our sample preparation. The DSL results showed similar particle diameters for those proteins. We are working on further analysis of XRCC4s with substitution of other serine sites to an aspartic acid aspartic and discuss on the XRCC4 activation mechanism.

[1]Williams, G.J. et al., DNA Repair 17, 110-120 (2014).
[2]Nishikubo, K. et al., The 23rd Hiroshima International Symposium on Synchrotron Radiation, 2019.
会議概要(会議名, 開催地, 会期, 主催者等)
内容記述タイプ Other
内容記述 第3回QST国際シンポジウム「Quantum Life Science」
発表年月日
日付 2019-12-04
日付タイプ Issued
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