Quantitative affinity interaction of ubiquitinated and non-ubiquitinated proteins with proteasome subunit Rpn10
- 作者: Buneeva O.1, Gnedenko O.1, Kopylov A.1, Medvedeva M.2, Zgoda V.1, Ivanov A.1, Medvedev A.1
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隶属关系:
- Orekhovich Institute of Biomedical Chemistry
- Lomonosov Moscow State University
- 期: 卷 82, 编号 9 (2017)
- 页面: 1042-1047
- 栏目: Article
- URL: https://journals.rcsi.science/0006-2979/article/view/151469
- DOI: https://doi.org/10.1134/S0006297917090073
- ID: 151469
如何引用文章
详细
Recent proteomic profiling of mouse brain preparations using the ubiquitin receptor, Rpn10 proteasome subunit, as an affinity ligand revealed a representative group of proteins bound to this sorbent (Medvedev, A. E., et al. (2017) Biochemistry (Moscow), 82, 330-339). In the present study, we investigated interaction of the Rpn10 subunit of proteasomes with some of these identified proteins: glyceraldehyde-3-phosphate dehydrogenase (GAPDH), pyruvate kinase, and histones H2A and H2B. The study revealed: (i) quantitative affinity interaction of the proteasome subunit immobilized on a Biacore-3000 optical biosensor cuvette with both the GAPDH (Kd = 2.4·10–6 M) and pyruvate kinase (Kd = 2.8·10–5 M); (ii) quantitative high-affinity interaction of immobilized histones H2A and H2B with the Rpn10 subunit (Kd values of 6.5·10–8 and 3.2·10–9 M, respectively). Mass spectrometric analysis revealed the presence of the ubiquitin signature (GG) only in a highly purified preparation of GAPDH. We suggest that binding (especially high-affinity binding) of non-ubiquitinated proteins to the Rpn10 proteasome subunit can both regulate the functioning of this proteasomal ubiquitin receptor (by competing with ubiquitinated substrates) and promote activation of other pathways for proteolytic degradation of proteins destined to the proteasome.
作者简介
O. Buneeva
Orekhovich Institute of Biomedical Chemistry
Email: professor57@yandex.ru
俄罗斯联邦, Moscow, 119121
O. Gnedenko
Orekhovich Institute of Biomedical Chemistry
Email: professor57@yandex.ru
俄罗斯联邦, Moscow, 119121
A. Kopylov
Orekhovich Institute of Biomedical Chemistry
Email: professor57@yandex.ru
俄罗斯联邦, Moscow, 119121
M. Medvedeva
Lomonosov Moscow State University
Email: professor57@yandex.ru
俄罗斯联邦, Moscow
V. Zgoda
Orekhovich Institute of Biomedical Chemistry
Email: professor57@yandex.ru
俄罗斯联邦, Moscow, 119121
A. Ivanov
Orekhovich Institute of Biomedical Chemistry
Email: professor57@yandex.ru
俄罗斯联邦, Moscow, 119121
A. Medvedev
Orekhovich Institute of Biomedical Chemistry
编辑信件的主要联系方式.
Email: professor57@yandex.ru
俄罗斯联邦, Moscow, 119121
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