{"id":57893,"date":"2026-11-11T14:10:53","date_gmt":"2026-11-11T14:10:53","guid":{"rendered":"https:\/\/matis.is\/?p=57893"},"modified":"2026-11-11T14:10:55","modified_gmt":"2026-11-11T14:10:55","slug":"structural-and-functional-characterization-of-a-hyperthermostable-single-stranded-dna-binding-protein-from-a-hot-spring-metagenome","status":"publish","type":"post","link":"https:\/\/matis.is\/en\/greinar\/structural-and-functional-characterization-of-a-hyperthermostable-single-stranded-dna-binding-protein-from-a-hot-spring-metagenome\/","title":{"rendered":"Structural and functional characterization of a hyperthermostable single-stranded DNA-binding protein from a hot spring metagenome"},"content":{"rendered":"<p class=\"wp-block-paragraph\">We present the structural and functional characterization of a single-stranded DNA-binding protein (SSB-M5) identified from a hot spring metagenome in Vatnaj\u00f6kull National Park, Iceland. This small protein (136 aa; 15,695 Da) shares 100% amino acid sequence identity with two previously uncharacterized SSBs from hyperthermophilic Fervidobacterium species. Functional complementation assay demonstrated that SSB-M5 can substitute for Escherichia coli SSB in an ssb<sup>\u2013<\/sup> mutant strain, confirming its biological activity. A recombinant C-terminally His-tagged SSB-M5 was overproduced, purified to homogeneity, and subjected to structural, biochemical, and biophysical analysis. The crystal structure revealed that SSB-M5 forms a dimer through a crystallographic twofold axis, with each monomer contributing to a large antiparallel \u03b2-sheet. The flat surfaces of the \u03b2-sheets from the two dimers are packed together via a second crystallographic twofold axis, forming a tetramer that serves as the functional unit of the SSB-M5. Electrophoretic mobility shift assays showed that SSB-M5, after heat treatment up to 100\u00b0C, forms stable DNA-protein complexes with the (dT)<sub>40<\/sub> oligo. Quantitative analyses revealed that SSB-M5 binds (dT)<sub>70<\/sub> oligonucleotide with very high affinity (K<sub>D<\/sub> = 72 \u00b1 6 pM). Hill analysis indicated cooperative binding, yielding an EC<sub>50<\/sub> of 141 pM and a Hill coefficient of 2. Moreover, inclusion of SSB-M5 in PCR reactions significantly enhanced amplification by eliminating non-specific products. Together, these findings identify SSB-M5 as a hyperthermostable, high-affinity single-stranded DNA-binding protein with potential applications in molecular biology and biotechnology.<\/p>","protected":false},"excerpt":{"rendered":"<p>We present the structural and functional characterization of a single-stranded DNA-binding protein (SSB-M5) identified from a hot spring metagenome in [&hellip;]<\/p>\n","protected":false},"author":7,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","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 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