Citation: Liang Lu-Jun, Si Yanyan, Tang Shan, Huang Dongliang, Wang Zhipeng A., Tian Changlin, Zheng Ji-Shen. Biochemical properties of K_{11, 48}-branched ubiquitin chains[J]. Chinese Chemical Letters, ;2018, 29(7): 1155-1159. doi: 10.1016/j.cclet.2018.03.022 shu

Biochemical properties of K_{11, 48}-branched ubiquitin chains

School of Life Sciences, University of Science and Technology of China, Hefei 230027, China

Corresponding author: Zheng Ji-Shen, jszheng@ustc.edu.cn
Received Date: 7 January 2018
Revised Date: 6 February 2018
Accepted Date: 19 March 2018
Available Online: 21 July 2018

Figures(4)

As one of the most widely existing post-translational modification models, ubiquitination regulates diverse cellular activities. In eukaryotes, K_{11, 48}-branched ubiquitin chains play key roles in cell cycle and protein quality control. However, the structural and biochemical properties of K_{11, 48}-branched ubiquitin chains have not been well examined. Here we employed the synthetic linkage-and length-defined K_{11, 48}-branched ubiquitin chains to examine their binding and hydrolysis properties in vitro. Quantitatively affinity determination of ubiquitin chains to the proteasome ubiquitin receptor S5a indicated that the S5a exhibited preference binding to K_{11, 48}-branched chains over K₁₁-linked chains, but not K₄₈-conjugated chains. In addition, deubiquitination experiments were carried out and the results showed that K_{11, 48}-branched chains were preferably hydrolyzed by proteasome-associated deubiquitinase Rpn11 than homotypic K₁₁ or K₄₈-linked chains.
- Post-translational modification,
- Ubiquitination,
- K_{11, 48}-branched chains,
- Affinity,
- Deubiquitination,
- Native chemical ligation of peptide,
- hydrazine
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沈阳化工大学材料科学与工程学院沈阳 110142

Biochemical properties of K11, 48-branched ubiquitin chains

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Biochemical properties of K_{11, 48}-branched ubiquitin chains