{"id":50247,"date":"2023-08-01T14:32:48","date_gmt":"2023-08-01T14:32:48","guid":{"rendered":"https:\/\/matis.is\/?p=50247"},"modified":"2023-08-01T14:32:49","modified_gmt":"2023-08-01T14:32:49","slug":"molecular-characterization-of-a-dna-polymerase-from-thermus-thermophilus-mat72-phage-vb_tt72-a-novel-type-a-family-enzyme-with-strong-proofreading-activity","status":"publish","type":"post","link":"https:\/\/matis.is\/en\/greinar\/molecular-characterization-of-a-dna-polymerase-from-thermus-thermophilus-mat72-phage-vb_tt72-a-novel-type-a-family-enzyme-with-strong-proofreading-activity\/","title":{"rendered":"Molecular Characterization of a DNA Polymerase from\u00a0<em>Thermus thermophilus<\/em>\u00a0MAT72 Phage vB_Tt72: A Novel Type-A Family Enzyme with Strong Proofreading Activity"},"content":{"rendered":"<p>We present a structural and functional analysis of the thermophilic DNA polymerase\u00a0<em>Thermus thermophilus<\/em>\u00a0MAT72 phage vB_Tt72. The enzyme shows low sequence identity (&lt;30%) to the members of the type-A family of DNA polymerases, except for two yet uncharacterized DNA polymerases of\u00a0<em>T. thermophilus<\/em>\u00a0phages: \u03c6YS40 (91%) and \u03c6TMA (90%). The Tt72\u00a0<em>polA<\/em>\u00a0gene does not complement the\u00a0<em>Escherichia coli<\/em>\u00a0<em>polA<\/em><sup>-<\/sup>\u00a0mutant in replicating\u00a0<em>polA<\/em>-dependent plasmid replicons. It encodes a 703-aa protein with a predicted molecular weight of 80,490 and an isoelectric point of 5.49. The enzyme contains a nucleotidyltransferase domain and a 3\u2032-5\u2032 exonuclease domain that is engaged in proofreading. Recombinant enzyme with His-tag at the\u00a0<em>N<\/em>-terminus was overproduced in\u00a0<em>E. coli<\/em>, subsequently purified by immobilized metal affinity chromatography, and biochemically characterized. The enzyme exists in solution in monomeric form and shows optimum activity at pH 8.5, 25 mM KCl, and 0.5 mM Mg<sup>2+<\/sup>. Site-directed analysis proved that highly conserved residues D15, E17, D78, D180, and D184 in 3\u2032-5\u2032 exonuclease and D384 and D615 in the nucleotidyltransferase domain are critical for the enzyme&#039;s activity. Despite the source of origin, the Tt72 DNA polymerase has not proven to be highly thermoresistant, with a temperature optimum at 55 \u00b0C. Above 60 \u00b0C, the rapid loss of function follows with no activity &gt; 75 \u00b0C. However, during heat treatment (10 min at 75 \u00b0C), trehalose, trimethylamine\u00a0<em>N<\/em>-oxide, and betaine protected the enzyme against thermal inactivation. A midpoint of thermal denaturation at T<sub>m<\/sub>\u00a0= 74.6 \u00b0C (\u0394H<sub>cal<\/sub>\u00a0= 2.05 \u00d7 10<sup>4<\/sup>\u00a0cal mol<sup>\u22121<\/sup>) and circular dichroism spectra &gt; 60 \u00b0C indicate the enzyme&#039;s moderate thermal stability.<\/p>","protected":false},"excerpt":{"rendered":"<p>We present a structural and functional analysis of the DNA polymerase of thermophilic\u00a0Thermus thermophilus\u00a0MAT72 phage vB_Tt72. The enzyme shows low [&hellip;]<\/p>\n","protected":false},"author":3,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"template-greinar.php","format":"standard","meta":{"_acf_changed":false,"_uag_custom_page_level_css":"","site-sidebar-layout":"default","site-content-layout":"","ast-site-content-layout":"default","site-content-style":"default","site-sidebar-style":"default","ast-global-header-display":"","ast-banner-title-visibility":"","ast-main-header-display":"","ast-hfb-above-header-display":"","ast-hfb-below-header-display":"","ast-hfb-mobile-header-display":"","site-post-title":"","ast-breadcrumbs-content":"","ast-featured-img":"","footer-sml-layout":"","ast-disable-related-posts":"","theme-transparent-header-meta":"","adv-header-id-meta":"","stick-header-meta":"","header-above-stick-meta":"","header-main-stick-meta":"","header-below-stick-meta":"","astra-migrate-meta-layouts":"default","ast-page-background-enabled":"default","ast-page-background-meta":{"desktop":{"background-color":"var(--ast-global-color-5)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"tablet":{"background-color":"","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"mobile":{"background-color":"","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""}},"ast-content-background-meta":{"desktop":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"tablet":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""},"mobile":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center center","background-size":"auto","background-attachment":"scroll","background-type":"","background-media":"","overlay-type":"","overlay-color":"","overlay-opacity":"","overlay-gradient":""}},"footnotes":""},"categories":[2011],"tags":[2167,2165,2166],"class_list":["post-50247","post","type-post","status-publish","format-standard","hentry","category-greinar","tag-3-5-exonuclease-activity","tag-dna-polymerase","tag-thermus-phage"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v27.4 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Molecular Characterization of a DNA Polymerase from\u00a0Thermus thermophilus\u00a0MAT72 Phage vB_Tt72: A Novel Type-A Family Enzyme with Strong Proofreading Activity - Mat\u00eds<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/matis.is\/en\/greinar\/molecular-characterization-of-a-dna-polymerase-from-thermus-thermophilus-mat72-phage-vb_tt72-a-novel-type-a-family-enzyme-with-strong-proofreading-activity\/\" \/>\n<meta property=\"og:locale\" content=\"en_GB\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Molecular Characterization of a DNA Polymerase from\u00a0Thermus thermophilus\u00a0MAT72 Phage vB_Tt72: A Novel Type-A Family Enzyme with Strong Proofreading Activity - Mat\u00eds\" \/>\n<meta property=\"og:description\" content=\"We present a structural and functional analysis of the DNA polymerase of thermophilic\u00a0Thermus thermophilus\u00a0MAT72 phage vB_Tt72. The enzyme shows low [&hellip;]\" \/>\n<meta property=\"og:url\" content=\"https:\/\/matis.is\/en\/greinar\/molecular-characterization-of-a-dna-polymerase-from-thermus-thermophilus-mat72-phage-vb_tt72-a-novel-type-a-family-enzyme-with-strong-proofreading-activity\/\" \/>\n<meta property=\"og:site_name\" content=\"Mat\u00eds\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/matisiceland\" \/>\n<meta property=\"article:published_time\" content=\"2023-08-01T14:32:48+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2023-08-01T14:32:49+00:00\" \/>\n<meta name=\"author\" content=\"Krist\u00edn Edda Gylfad\u00f3ttir\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@matisiceland\" \/>\n<meta name=\"twitter:site\" content=\"@matisiceland\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Krist\u00edn Edda Gylfad\u00f3ttir\" \/>\n\t<meta name=\"twitter:label2\" content=\"Estimated reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"2 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\\\/\\\/schema.org\",\"@graph\":[{\"@type\":\"Article\",\"@id\":\"https:\\\/\\\/matis.is\\\/en\\\/greinar\\\/molecular-characterization-of-a-dna-polymerase-from-thermus-thermophilus-mat72-phage-vb_tt72-a-novel-type-a-family-enzyme-with-strong-proofreading-activity\\\/#article\",\"isPartOf\":{\"@id\":\"https:\\\/\\\/matis.is\\\/en\\\/greinar\\\/molecular-characterization-of-a-dna-polymerase-from-thermus-thermophilus-mat72-phage-vb_tt72-a-novel-type-a-family-enzyme-with-strong-proofreading-activity\\\/\"},\"author\":{\"name\":\"Krist\u00edn Edda Gylfad\u00f3ttir\",\"@id\":\"https:\\\/\\\/matis.is\\\/#\\\/schema\\\/person\\\/af2d479c72e5e79c4570d409abf2dc9b\"},\"headline\":\"Molecular Characterization of a DNA Polymerase from\u00a0Thermus thermophilus\u00a0MAT72 Phage vB_Tt72: A Novel Type-A Family Enzyme with Strong Proofreading Activity\",\"datePublished\":\"2023-08-01T14:32:48+00:00\",\"dateModified\":\"2023-08-01T14:32:49+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\\\/\\\/matis.is\\\/en\\\/greinar\\\/molecular-characterization-of-a-dna-polymerase-from-thermus-thermophilus-mat72-phage-vb_tt72-a-novel-type-a-family-enzyme-with-strong-proofreading-activity\\\/\"},\"wordCount\":267,\"publisher\":{\"@id\":\"https:\\\/\\\/matis.is\\\/#organization\"},\"keywords\":[\"3\u2032-5\u2032 exonuclease activity\",\"DNA polymerase\",\"Thermus phage\"],\"articleSection\":[\"Greinar\"],\"inLanguage\":\"en-GB\"},{\"@type\":\"WebPage\",\"@id\":\"https:\\\/\\\/matis.is\\\/en\\\/greinar\\\/molecular-characterization-of-a-dna-polymerase-from-thermus-thermophilus-mat72-phage-vb_tt72-a-novel-type-a-family-enzyme-with-strong-proofreading-activity\\\/\",\"url\":\"https:\\\/\\\/matis.is\\\/en\\\/greinar\\\/molecular-characterization-of-a-dna-polymerase-from-thermus-thermophilus-mat72-phage-vb_tt72-a-novel-type-a-family-enzyme-with-strong-proofreading-activity\\\/\",\"name\":\"Molecular Characterization of a DNA Polymerase from\u00a0Thermus thermophilus\u00a0MAT72 Phage vB_Tt72: A Novel Type-A Family Enzyme with Strong Proofreading Activity - 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