Monomer unfolding of a bacterial ESCRT-III superfamily member is coupled to oligomer disassembly.

IF 4.5 3区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Protein Science Pub Date : 2024-11-01 DOI:10.1002/pro.5187
Ndjali Quarta, Tika Ram Bhandari, Martin Girard, Nadja Hellmann, Dirk Schneider
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引用次数: 0

Abstract

The inner membrane associated protein of 30 kDa (IM30), a member of the endosomal sorting complex required for transport (ESCRT-III) superfamily, is crucially involved in the biogenesis and maintenance of thylakoid membranes in cyanobacteria and chloroplasts. In solution, IM30 assembles into various large oligomeric barrel- or tube-like structures, whereas upon membrane binding it forms large, flat carpet structures. Dynamic localization of the protein in solution, to membranes and changes of the oligomeric states are crucial for its in vivo function. ESCRT-III proteins are known to form oligomeric structures that are dynamically assembled from monomeric/smaller oligomeric proteins, and thus these smaller building blocks must be assembled sequentially in a highly orchestrated manner, a still poorly understood process. The impact of IM30 oligomerization on function remains difficult to study due to its high intrinsic tendency to homo-oligomerize. Here, we used molecular dynamics simulations to investigate the stability of individual helices in IM30 and identified unstable regions that may provide structural flexibility. Urea-mediated disassembly of the IM30 barrel structures was spectroscopically monitored, as well as changes in the protein's tertiary and secondary structure. The experimental data were finally compared to a three-state model that describes oligomer disassembly and monomer unfolding. In this study, we identified a highly stable conserved structural core of ESCRT-III proteins and discuss the advantages of having flexible intermediate structures and their putative relevance for ESCRT-III proteins.

细菌 ESCRT-III 超家族成员的单体折叠与寡聚体解体相关联。
30 kDa 的内膜相关蛋白(IM30)是运输所需的内体分选复合体(ESCRT-III)超家族的成员,在蓝藻和叶绿体的类木质膜的生物形成和维持过程中起着至关重要的作用。在溶液中,IM30 组装成各种大型寡聚桶状或管状结构,而在与膜结合后,则形成大型扁平地毯结构。该蛋白质在溶液中、膜上的动态定位以及低聚物状态的变化对其体内功能至关重要。众所周知,ESCRT-III 蛋白形成的低聚物结构是由单体/较小的低聚物动态组装而成的,因此这些较小的构件必须以高度协调的方式按顺序组装,而这一过程至今仍鲜为人知。由于 IM30 本身具有高度的同源寡聚倾向,因此其寡聚化对功能的影响仍然难以研究。在这里,我们利用分子动力学模拟研究了 IM30 中单个螺旋的稳定性,并确定了可能提供结构灵活性的不稳定区域。通过光谱监测了尿素介导的 IM30 桶状结构的分解,以及蛋白质三级和二级结构的变化。最后将实验数据与描述低聚物分解和单体展开的三态模型进行了比较。在这项研究中,我们确定了 ESCRT-III 蛋白高度稳定的保守结构核心,并讨论了灵活的中间结构的优势及其与 ESCRT-III 蛋白的相关性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Protein Science
Protein Science 生物-生化与分子生物学
CiteScore
12.40
自引率
1.20%
发文量
246
审稿时长
1 months
期刊介绍: Protein Science, the flagship journal of The Protein Society, is a publication that focuses on advancing fundamental knowledge in the field of protein molecules. The journal welcomes original reports and review articles that contribute to our understanding of protein function, structure, folding, design, and evolution. Additionally, Protein Science encourages papers that explore the applications of protein science in various areas such as therapeutics, protein-based biomaterials, bionanotechnology, synthetic biology, and bioelectronics. The journal accepts manuscript submissions in any suitable format for review, with the requirement of converting the manuscript to journal-style format only upon acceptance for publication. Protein Science is indexed and abstracted in numerous databases, including the Agricultural & Environmental Science Database (ProQuest), Biological Science Database (ProQuest), CAS: Chemical Abstracts Service (ACS), Embase (Elsevier), Health & Medical Collection (ProQuest), Health Research Premium Collection (ProQuest), Materials Science & Engineering Database (ProQuest), MEDLINE/PubMed (NLM), Natural Science Collection (ProQuest), and SciTech Premium Collection (ProQuest).
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