{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["475(1)"],"submitter":["Vidhyasagar V"],"pubmed_abstract":["Human nucleic acid-binding protein 1 and 2 (hNABP1 and hNABP2, also known as hSSB2 and hSSB1 respectively) form two separate and independent complexes with two identical proteins, integrator complex subunit 3 (INTS3) and C9ORF80. We and other groups have demonstrated that hNABP1 and 2 are single-stranded (ss) DNA- and RNA-binding proteins, and function in DNA repair; however, the function of INTS3 and C9OFR80 remains elusive. In the present study, we purified recombinant proteins INTS3 and C9ORF80 to near homogeneity. Both proteins exist as a monomer in solution; however, C9ORF80 exhibits anomalous behavior on SDS-PAGE and gel filtration because of 48% random coil present in the protein. Using electrophoretic mobility shift assay (EMSA), INTS3 displays higher affinity toward ssRNA than ssD"],"journal":["The Biochemical journal"],"pagination":["45-60"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5748837"],"repository":["biostudies-literature"],"pubmed_title":["Biochemical characterization of INTS3 and C9ORF80, two subunits of hNABP1/2 heterotrimeric complex in nucleic acid binding."],"pmcid":["PMC5748837"],"pubmed_authors":["Guo M","Yadav M","Vidhyasagar V","He Y","Talwar T","Singh RS","Vizeacoumar FJ","Lukong KE","Katselis G","Wu Y"],"additional_accession":[]},"is_claimable":false,"name":"Biochemical characterization of INTS3 and C9ORF80, two subunits of hNABP1/2 heterotrimeric complex in nucleic acid binding.","description":"Human nucleic acid-binding protein 1 and 2 (hNABP1 and hNABP2, also known as hSSB2 and hSSB1 respectively) form two separate and independent complexes with two identical proteins, integrator complex subunit 3 (INTS3) and C9ORF80. We and other groups have demonstrated that hNABP1 and 2 are single-stranded (ss) DNA- and RNA-binding proteins, and function in DNA repair; however, the function of INTS3 and C9OFR80 remains elusive. In the present study, we purified recombinant proteins INTS3 and C9ORF80 to near homogeneity. Both proteins exist as a monomer in solution; however, C9ORF80 exhibits anomalous behavior on SDS-PAGE and gel filtration because of 48% random coil present in the protein. Using electrophoretic mobility shift assay (EMSA), INTS3 displays higher affinity toward ssRNA than ssD","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Jan","modification":"2026-05-05T21:17:35.173Z","creation":"2019-03-27T03:06:06Z"},"accession":"S-EPMC5748837","cross_references":{"pubmed":["29150435"],"doi":["10.1042/BCJ20170351"]}}