RING-type ubiquitin ligase McCPN1 catalyzes UBC8-dependent protein ubiquitination and interacts with Argonaute 4 in halophyte ice plant
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- 作者：Chang-Hua Lia ; 2 ; chosal_li@hotmail.com" class="auth_mail ; Chih-Pin Chianga ; 2 ; ls_8771121@yahoo.com.tw" class="auth_mail ; Jun-Yi Yangb ; jyang@nchu.edu.tw" class="auth_mail ; Chia-Jou Maa ; asuka128@yahoo.com.tw" class="auth_mail ; Yu-Chan Chena ; 1 ; hippocampus6@hotmail.com" class="auth_mail ; Hungchen Emilie Yena ; heyen@dragon.nchu.edu.tw" class="auth_mail
- 关键词：Argonaute 4 ; Copine ; In vitro enzyme assay ; Post-translational modification ; RING-type ubiquitin ligase ; Ubiquitin-conjugating enzyme
- 刊名：Plant Physiology and Biochemistry
- 出版年：July 2014
- 年：2014
- 卷：80
- 期：Complete
- 页码：211-219
- 全文大小：1347 K
文摘
- istitem" id="list_ulist0010">
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id="p0010">The RING-type E3 McCPN1 possesses selected E2-dependent ubiquitin ligase activity.
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id="p0015">McCPN1 localizes primarily on the plasma membrane and nucleus.
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id="p0020">The accumulation of McCPN1 increases in salt-stressed ice plant roots.
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id="p0025">Nuclear-localized protein Argonaute 4 is a McCPN1-interacting partner.