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本文引用的文献

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E1- and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea.E1- 和泛素样蛋白在古菌中提供了蛋白质连接和硫转移之间的直接联系。
Proc Natl Acad Sci U S A. 2011 Mar 15;108(11):4417-22. doi: 10.1073/pnas.1018151108. Epub 2011 Feb 28.
2
SAMPyling proteins in archaea.古菌中的 SAMPyling 蛋白。
Trends Biochem Sci. 2010 Jun;35(6):348-51. doi: 10.1016/j.tibs.2010.03.003. Epub 2010 May 23.
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More modifiers move on DNA damage.更多的修饰物在 DNA 损伤上移动。
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Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii.火烈球菌中的泛素样小 archaeal 修饰蛋白（SAMPs）。
Nature. 2010 Jan 7;463(7277):54-60. doi: 10.1038/nature08659.
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A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa.原核生物类泛素蛋白（Pup）的一个独特结构区域被蛋白酶体ATP酶Mpa的N端结构域识别。
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Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein.Pup是一种原核生物类泛素蛋白，是一种内在无序蛋白。
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Proteasomal components required for cell growth and stress responses in the haloarchaeon Haloferax volcanii.嗜盐古菌沃氏嗜盐碱杆菌中细胞生长和应激反应所需的蛋白酶体成分。
J Bacteriol. 2008 Dec;190(24):8096-105. doi: 10.1128/JB.01180-08. Epub 2008 Oct 17.
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Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis.参与结核分枝杆菌蛋白酶体途径的类泛素蛋白。
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Clustal W and Clustal X version 2.0.Clustal W和Clustal X 2.0版本
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来自沃氏嗜盐碱杆菌的泛素样小修饰蛋白（SAMP1）的离子强度依赖构象。

Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP1) from Haloferax volcanii.

机构信息

Hefei National Laboratory for Physical Sciences at Microscale, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.

出版信息

Protein Sci. 2013 Sep;22(9):1174-82. doi: 10.1002/pro.2302. Epub 2013 Jul 22.

DOI:10.1002/pro.2302
PMID:23818097
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3776330/
Abstract

Eukaryotic ubiquitin and ubiquitin-like systems play crucial roles in various cellular biological processes. In this work, we determined the solution structure of SAMP1 from Haloferax volcanii by NMR spectroscopy. Under low ionic conditions, SAMP1 presented two distinct conformations, one folded β-grasp and the other disordered. Interestingly, SAMP1 underwent a conformational conversion from disorder to order with ion concentration increasing, indicating that the ordered conformation is the functional form of SAMP1 under the physiological condition of H. volcanii. Furthermore, SAMP1 could interact with proteasome-activating nucleotidase B, supposing a potential role of SAMP1 in the protein degradation pathway mediated by proteasome.

摘要

真核生物的泛素和泛素样系统在各种细胞生物学过程中发挥着关键作用。在这项工作中，我们通过 NMR 光谱法测定了来自火烈球菌的 SAMP1 的溶液结构。在低离子条件下，SAMP1 呈现出两种不同的构象，一种折叠的 β-抓握构象，另一种无序构象。有趣的是，SAMP1 随着离子浓度的增加从无序到有序发生构象转换，这表明在 H. volcanii 的生理条件下，有序构象是 SAMP1 的功能形式。此外，SAMP1 可以与蛋白酶体激活核苷酸酶 B 相互作用，这表明 SAMP1 在蛋白酶体介导的蛋白质降解途径中可能发挥作用。