Structure and Function of the RING Domains of RNF20 and RNF40, Dimeric E3 Ligases that Monoubiquitylate Histone H2B
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- 作者：Martina Foglizzo ; Adam J. Middleton ; Catherine L. Day ; catherine.day@otago.ac.nz" class="auth_mail" title="E-mail the corresponding author
- 关键词：BIRC7 ; baculoviral IAP repeat-containing protein 7 ; cIAP ; cellular IAP ; E2 ; ~ ; Ub ; E2 enzyme conjugated to ubiquitin ; HADDOCK ; high ambiguity driven protein&ndash ; protein docking ; IAP ; inhibitor of apoptosis ; MALLS ; multi-angle laser light scattering ; MDM ; mouse double minute ; PBS ; phosphate-buffered saline ; R6BD ; Rad6-binding domain ; RING ; really interesting new gene ; RNF ; RING finger protein ; UBC ; ubiquitin-conjugating domain ; ubH2B ; monoubiquitylation of histone H2B ; XIAP ; X chromosom
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：9 October 2016
- 年：2016
- 卷：428
- 期：20
- 页码：4073-4086
- 全文大小：5054 K
文摘
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RNF20 and Ube2B monoubiquitylate histone H2B at K120 for transcriptional activation.
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The RING domain of RNF20 promotes ubiquitin transfer by Ube2B.
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Key contacts favor the interaction between RNF20 and Ube2B~Ub.
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The RNF20 and RNF40 RING domains form a functional heterodimer.
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The RNF20–Ube2B~Ub model provides an initial framework to understand how the modification of histone H2B at K120 is mediated.