Julian A. Barden, Paul M.G. Curmi, Cristobal G. Dos Remedios
{"title":"晶体肌动蛋白管","authors":"Julian A. Barden, Paul M.G. Curmi, Cristobal G. Dos Remedios","doi":"10.1016/0005-2795(81)90089-1","DOIUrl":null,"url":null,"abstract":"<div><p>The effect of the trivalent cations scandium (Sc<sup>3+</sup>) and yttrium (Y<sup>3+</sup>) on the conformation of G-actin was examined using ultraviolet difference and high resolution <sup>1</sup>H-NMR spectroscopy. A comparison was made with data obtained previously with the trivalent lanthanide cations (Ln<sup>3+</sup>). These results indicate that the first and subsequent Y ions (ionic radius 101.9 pm) behave exactly like Ln<sup>3+</sup>. Sc<sup>3+</sup> is a smaller ion (87 pm) than any of the Ln<sup>3+</sup>. The first Sc<sup>3+</sup> binds to a site on actin that is inaccessible to Mg<sup>2+</sup>, Y<sup>3+</sup> and Ln<sup>3+</sup>. However, the second Sc<sup>3+</sup> to bind behaves like an Ln<sup>3+</sup>. On replacing the native divalent cation (Mg<sup>2+</sup>), both Y<sup>3+</sup> and Sc<sup>3+</sup> mobilize the adenine ring of ATP bound to actin, thus exposing underlying residues to the solvent. When Y<sup>3+</sup> and Sc<sup>3+</sup> saturate their binding sites on actin, and when the ionic strength is raised to 0.1 M with KCI at pH 6.9, the actin aggregates. Y<sup>3+</sup> binds to actin with a ratio of 6 : 1 and induces the aggregation of actin into crystalline actin tubes, whilstSc<sup>3+</sup> Sc<sup>3+</sup>binds with a ratio of 8 : 1 and induces amorphous actin aggregates. These results are consistent with the suggestion that actin tubes are induced by trivalent cations, principally on the basis of their binding stoichiometry, which in turn is determined by ionic radius.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":"671 1","pages":"Pages 25-32"},"PeriodicalIF":0.0000,"publicationDate":"1981-11-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90089-1","citationCount":"8","resultStr":"{\"title\":\"Crystalline actin tubes\",\"authors\":\"Julian A. Barden, Paul M.G. Curmi, Cristobal G. Dos Remedios\",\"doi\":\"10.1016/0005-2795(81)90089-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The effect of the trivalent cations scandium (Sc<sup>3+</sup>) and yttrium (Y<sup>3+</sup>) on the conformation of G-actin was examined using ultraviolet difference and high resolution <sup>1</sup>H-NMR spectroscopy. A comparison was made with data obtained previously with the trivalent lanthanide cations (Ln<sup>3+</sup>). These results indicate that the first and subsequent Y ions (ionic radius 101.9 pm) behave exactly like Ln<sup>3+</sup>. Sc<sup>3+</sup> is a smaller ion (87 pm) than any of the Ln<sup>3+</sup>. The first Sc<sup>3+</sup> binds to a site on actin that is inaccessible to Mg<sup>2+</sup>, Y<sup>3+</sup> and Ln<sup>3+</sup>. However, the second Sc<sup>3+</sup> to bind behaves like an Ln<sup>3+</sup>. On replacing the native divalent cation (Mg<sup>2+</sup>), both Y<sup>3+</sup> and Sc<sup>3+</sup> mobilize the adenine ring of ATP bound to actin, thus exposing underlying residues to the solvent. When Y<sup>3+</sup> and Sc<sup>3+</sup> saturate their binding sites on actin, and when the ionic strength is raised to 0.1 M with KCI at pH 6.9, the actin aggregates. Y<sup>3+</sup> binds to actin with a ratio of 6 : 1 and induces the aggregation of actin into crystalline actin tubes, whilstSc<sup>3+</sup> Sc<sup>3+</sup>binds with a ratio of 8 : 1 and induces amorphous actin aggregates. These results are consistent with the suggestion that actin tubes are induced by trivalent cations, principally on the basis of their binding stoichiometry, which in turn is determined by ionic radius.</p></div>\",\"PeriodicalId\":100165,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure\",\"volume\":\"671 1\",\"pages\":\"Pages 25-32\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-11-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0005-2795(81)90089-1\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Protein Structure\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0005279581900891\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005279581900891","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The effect of the trivalent cations scandium (Sc3+) and yttrium (Y3+) on the conformation of G-actin was examined using ultraviolet difference and high resolution 1H-NMR spectroscopy. A comparison was made with data obtained previously with the trivalent lanthanide cations (Ln3+). These results indicate that the first and subsequent Y ions (ionic radius 101.9 pm) behave exactly like Ln3+. Sc3+ is a smaller ion (87 pm) than any of the Ln3+. The first Sc3+ binds to a site on actin that is inaccessible to Mg2+, Y3+ and Ln3+. However, the second Sc3+ to bind behaves like an Ln3+. On replacing the native divalent cation (Mg2+), both Y3+ and Sc3+ mobilize the adenine ring of ATP bound to actin, thus exposing underlying residues to the solvent. When Y3+ and Sc3+ saturate their binding sites on actin, and when the ionic strength is raised to 0.1 M with KCI at pH 6.9, the actin aggregates. Y3+ binds to actin with a ratio of 6 : 1 and induces the aggregation of actin into crystalline actin tubes, whilstSc3+ Sc3+binds with a ratio of 8 : 1 and induces amorphous actin aggregates. These results are consistent with the suggestion that actin tubes are induced by trivalent cations, principally on the basis of their binding stoichiometry, which in turn is determined by ionic radius.