钙和钠介导的中间丝状蛋白FilP的动态组装。

IF 1 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY Protein and Peptide Letters Pub Date : 2023-01-01 DOI:10.2174/0929866530666221209120300
Caihong Fu, Shanshan Zhang, Fan Yang, Ximing Chen, Xiuxia Sun
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引用次数: 0

摘要

背景:细胞骨架元件在细胞形态、细胞分裂、细胞迁移和DNA分裂中发挥着关键作用。在链霉菌中发现了if样蛋白FilP,它通过为细胞提供直接的机械支持,在结构上起着重要的细胞骨架作用。目的:研究不同条件下影响FilP聚合的因素。方法:采用DLS技术实时监测彩色链霉菌FilP的体外组装过程。结果:少量的二价阳离子(如CaCl2或MgCl2)的存在促进了FilP的聚合,而大量的二价阳离子则抑制其聚合。此外,高浓度的NaCl、KCl、NH4Cl和KNO3均抑制了FilP的聚合。EDTA对FilP的聚合有很强的抑制作用,即使随后加入Ca2+也不能启动FilP的组装。FilP在pH 6 ~ pH 8范围内发生聚合,聚合度对pH值敏感,中性pH下FilP形成网状条纹细丝,而pH 8和pH 6时FilP细丝更加无序或松散堆积。结论:FilP的组装是钙介导的。Ca2+不仅是FilP聚合所必需的,也是FilP维持高阶聚合物结构所必需的。Ca2+的促进作用和Na+的抑制作用在广泛的条件下持续存在,这表明FilP可能利用钙和钠离子作为介导其聚合过程的一般机制。
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Calcium and Sodium-mediated Dynamic Assembly of Intermediate Filament-like Protein FilP.

Background: Cytoskeletal elements play key roles in cell morphology, cell division, cell mobility, and DNA partitioning in all domains of life. The IF-like protein FilP was discovered in Streptomyces coelicolor, and it was found to perform a structurally important cytoskeletal role by providing direct mechanical support for the cells.

Objective: This work investigated the factors influencing FilP polymerization under a variety of conditions.

Methods: DLS technique was applied to real-time monitor the in vitro assembly process of Streptomyces coelicolor FilP.

Results: The presence of small amounts of divalent cations, such as CaCl2 or MgCl2, enhanced the polymerization of FilP, while higher amounts suppressed its polymerization. Moreover, high concentrations of NaCl, KCl, NH4Cl, and KNO3 both suppressed the polymerization of FilP. EDTA was found to have a very prohibitive effect on FilP polymerization, and even the following addition of Ca2+ could not initiate the assembly of FilP. FilP polymerized under a range of pHs ranging from pH 6 to pH 8, while the polymerization degree was sensitive to pH. FilP formed network-like, striated filaments at neutral pH, while the filaments became more disordered or loosely packed at pH 8 and pH 6, respectively.

Conclusion: FilP assembly is calcium-mediated. Ca2+ is not only required for FilP polymerization, but also required for FilP to maintain the higher-order polymer structure. The accelerative effect of Ca2+ and the suppressive effect of Na+ persisted under a wide range of conditions, suggesting that FilP might use calcium and sodium ions as a general mechanism to mediate its polymerization process.

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来源期刊
Protein and Peptide Letters
Protein and Peptide Letters 生物-生化与分子生物学
CiteScore
2.90
自引率
0.00%
发文量
98
审稿时长
2 months
期刊介绍: Protein & Peptide Letters publishes letters, original research papers, mini-reviews and guest edited issues in all important aspects of protein and peptide research, including structural studies, advances in recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, and drug design. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallization and preliminary structure determination of biologically important proteins are considered only if they include significant new approaches or deal with proteins of immediate importance, and preliminary structure determinations of biologically important proteins. Purely theoretical/review papers should provide new insight into the principles of protein/peptide structure and function. Manuscripts describing computational work should include some experimental data to provide confirmation of the results of calculations. Protein & Peptide Letters focuses on: Structure Studies Advances in Recombinant Expression Drug Design Chemical Synthesis Function Pharmacology Enzymology Conformational Analysis Immunology Biotechnology Protein Engineering Protein Folding Sequencing Molecular Recognition Purification and Analysis
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