Expression in Escherichia coli, purification and characterization of LRSAM1, a LRR and RING domain E3 ubiquitin ligase
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- 作者：Yanmin Guo1 ; Weixiang Bian1 ; Yuan Zhang ; Hongtao Li ; htli@swu.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：LRSAM1 ; Ubiquitin ligase ; RING-finger ; Purification ; Activity
- 刊名：Protein Expression and Purification
- 出版年：2017
- 出版时间：January 2017
- 年：2017
- 卷：129
- 期：Complete
- 页码：158-161
- 全文大小：915 K
文摘
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LRSAM1 was expressed at high level in Escherichia.coli as inclusion bodies.
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LRSAM1 was purified from inclusion bodies through denaturation, renaturation and ammonium sulfate precipitation steps.
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The E3 activity of LRSAM1 was pH-dependent in cooperation with UbcH5-type E2-enzymes.
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LRSAM1-driven ubiquitination favored K6-, K27-, K29- and K48-linkages.
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