Caihong Fu, Shanshan Zhang, Fan Yang, Ximing Chen, Xiuxia Sun
{"title":"钙和钠介导的中间丝状蛋白FilP的动态组装。","authors":"Caihong Fu, Shanshan Zhang, Fan Yang, Ximing Chen, Xiuxia Sun","doi":"10.2174/0929866530666221209120300","DOIUrl":null,"url":null,"abstract":"<p><strong>Background: </strong>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.</p><p><strong>Objective: </strong>This work investigated the factors influencing FilP polymerization under a variety of conditions.</p><p><strong>Methods: </strong>DLS technique was applied to real-time monitor the in vitro assembly process of Streptomyces coelicolor FilP.</p><p><strong>Results: </strong>The presence of small amounts of divalent cations, such as CaCl<sub>2</sub> or MgCl<sub>2</sub>, enhanced the polymerization of FilP, while higher amounts suppressed its polymerization. Moreover, high concentrations of NaCl, KCl, NH<sub>4</sub>Cl, and KNO<sub>3</sub> both suppressed the polymerization of FilP. EDTA was found to have a very prohibitive effect on FilP polymerization, and even the following addition of Ca<sup>2+</sup> 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.</p><p><strong>Conclusion: </strong>FilP assembly is calcium-mediated. Ca<sup>2+</sup> is not only required for FilP polymerization, but also required for FilP to maintain the higher-order polymer structure. The accelerative effect of Ca<sup>2+</sup> and the suppressive effect of Na<sup>+</sup> 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.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":"30 2","pages":"154-161"},"PeriodicalIF":1.0000,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Calcium and Sodium-mediated Dynamic Assembly of Intermediate Filament-like Protein FilP.\",\"authors\":\"Caihong Fu, Shanshan Zhang, Fan Yang, Ximing Chen, Xiuxia Sun\",\"doi\":\"10.2174/0929866530666221209120300\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><strong>Background: </strong>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.</p><p><strong>Objective: </strong>This work investigated the factors influencing FilP polymerization under a variety of conditions.</p><p><strong>Methods: </strong>DLS technique was applied to real-time monitor the in vitro assembly process of Streptomyces coelicolor FilP.</p><p><strong>Results: </strong>The presence of small amounts of divalent cations, such as CaCl<sub>2</sub> or MgCl<sub>2</sub>, enhanced the polymerization of FilP, while higher amounts suppressed its polymerization. Moreover, high concentrations of NaCl, KCl, NH<sub>4</sub>Cl, and KNO<sub>3</sub> both suppressed the polymerization of FilP. EDTA was found to have a very prohibitive effect on FilP polymerization, and even the following addition of Ca<sup>2+</sup> 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.</p><p><strong>Conclusion: </strong>FilP assembly is calcium-mediated. Ca<sup>2+</sup> is not only required for FilP polymerization, but also required for FilP to maintain the higher-order polymer structure. The accelerative effect of Ca<sup>2+</sup> and the suppressive effect of Na<sup>+</sup> 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.</p>\",\"PeriodicalId\":20736,\"journal\":{\"name\":\"Protein and Peptide Letters\",\"volume\":\"30 2\",\"pages\":\"154-161\"},\"PeriodicalIF\":1.0000,\"publicationDate\":\"2023-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Protein and Peptide Letters\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.2174/0929866530666221209120300\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Protein and Peptide Letters","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.2174/0929866530666221209120300","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
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.
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