date: 2023-02-07T10:53:11Z
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pdf:docinfo:title: Insight into the Structural Basis for Dual Nucleic Acid?Recognition by the Scaffold Attachment FactorB2 Protein
xmp:CreatorTool: LaTeX with hyperref
Keywords: scaffold attachment factor proteins; nuclear matrix; nuclear magnetic resonancespectroscopy; SAP domain; RRM domain; dual nucleic acid binding; chromatin; RNA processing; protein dynamics
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subject: The family of scaffold attachment factor B (SAFB) proteins comprises three members and was first identified as binders of the nuclear matrix/scaffold. Over the past two decades, SAFBs were shown to act in DNA repair, mRNA/(l)ncRNA processing and as part of protein complexes with chromatin-modifying enzymes. SAFB proteins are approximately 100 kDa-sized dual nucleic acid-binding proteins with dedicated domains in an otherwise largely unstructured context, but whether and how they discriminate DNA and RNA binding has remained enigmatic. We here provide the SAFB2 DNA- and RNA-binding SAP and RRM domains in their functional boundaries and use solution NMR spectroscopy to ascribe DNA- and RNA-binding functions. We give insight into their target nucleic acid preferences and map the interfaces with respective nucleic acids on sparse data-derived SAP and RRM domain structures. Further, we provide evidence that the SAP domain exhibits intra-domain dynamics and a potential tendency to dimerize, which may expand its specifically targeted DNA sequence range. Our data provide a first molecular basis of and a starting point towards deciphering DNA- and RNA-binding functions of SAFB2 on the molecular level and serve a basis for understanding its localization to specific regions of chromatin and its involvement in the processing of specific RNA species.
dc:creator: Sophie M. Korn, Julian Von Ehr, Karthikeyan Dhamotharan, Jan-Niklas Tants, Rupert Abele and Andreas Schlundt
dcterms:created: 2023-02-07T10:46:20Z
Last-Modified: 2023-02-07T10:53:11Z
dcterms:modified: 2023-02-07T10:53:11Z
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title: Insight into the Structural Basis for Dual Nucleic Acid?Recognition by the Scaffold Attachment FactorB2 Protein
Last-Save-Date: 2023-02-07T10:53:11Z
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pdf:docinfo:keywords: scaffold attachment factor proteins; nuclear matrix; nuclear magnetic resonancespectroscopy; SAP domain; RRM domain; dual nucleic acid binding; chromatin; RNA processing; protein dynamics
pdf:docinfo:modified: 2023-02-07T10:53:11Z
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dc:title: Insight into the Structural Basis for Dual Nucleic Acid?Recognition by the Scaffold Attachment FactorB2 Protein
modified: 2023-02-07T10:53:11Z
cp:subject: The family of scaffold attachment factor B (SAFB) proteins comprises three members and was first identified as binders of the nuclear matrix/scaffold. Over the past two decades, SAFBs were shown to act in DNA repair, mRNA/(l)ncRNA processing and as part of protein complexes with chromatin-modifying enzymes. SAFB proteins are approximately 100 kDa-sized dual nucleic acid-binding proteins with dedicated domains in an otherwise largely unstructured context, but whether and how they discriminate DNA and RNA binding has remained enigmatic. We here provide the SAFB2 DNA- and RNA-binding SAP and RRM domains in their functional boundaries and use solution NMR spectroscopy to ascribe DNA- and RNA-binding functions. We give insight into their target nucleic acid preferences and map the interfaces with respective nucleic acids on sparse data-derived SAP and RRM domain structures. Further, we provide evidence that the SAP domain exhibits intra-domain dynamics and a potential tendency to dimerize, which may expand its specifically targeted DNA sequence range. Our data provide a first molecular basis of and a starting point towards deciphering DNA- and RNA-binding functions of SAFB2 on the molecular level and serve a basis for understanding its localization to specific regions of chromatin and its involvement in the processing of specific RNA species.
pdf:docinfo:subject: The family of scaffold attachment factor B (SAFB) proteins comprises three members and was first identified as binders of the nuclear matrix/scaffold. Over the past two decades, SAFBs were shown to act in DNA repair, mRNA/(l)ncRNA processing and as part of protein complexes with chromatin-modifying enzymes. SAFB proteins are approximately 100 kDa-sized dual nucleic acid-binding proteins with dedicated domains in an otherwise largely unstructured context, but whether and how they discriminate DNA and RNA binding has remained enigmatic. We here provide the SAFB2 DNA- and RNA-binding SAP and RRM domains in their functional boundaries and use solution NMR spectroscopy to ascribe DNA- and RNA-binding functions. We give insight into their target nucleic acid preferences and map the interfaces with respective nucleic acids on sparse data-derived SAP and RRM domain structures. Further, we provide evidence that the SAP domain exhibits intra-domain dynamics and a potential tendency to dimerize, which may expand its specifically targeted DNA sequence range. Our data provide a first molecular basis of and a starting point towards deciphering DNA- and RNA-binding functions of SAFB2 on the molecular level and serve a basis for understanding its localization to specific regions of chromatin and its involvement in the processing of specific RNA species.
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pdf:docinfo:creator: Sophie M. Korn, Julian Von Ehr, Karthikeyan Dhamotharan, Jan-Niklas Tants, Rupert Abele and Andreas Schlundt
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creator: Sophie M. Korn, Julian Von Ehr, Karthikeyan Dhamotharan, Jan-Niklas Tants, Rupert Abele and Andreas Schlundt
meta:author: Sophie M. Korn, Julian Von Ehr, Karthikeyan Dhamotharan, Jan-Niklas Tants, Rupert Abele and Andreas Schlundt
dc:subject: scaffold attachment factor proteins; nuclear matrix; nuclear magnetic resonancespectroscopy; SAP domain; RRM domain; dual nucleic acid binding; chromatin; RNA processing; protein dynamics
meta:creation-date: 2023-02-07T10:46:20Z
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meta:keyword: scaffold attachment factor proteins; nuclear matrix; nuclear magnetic resonancespectroscopy; SAP domain; RRM domain; dual nucleic acid binding; chromatin; RNA processing; protein dynamics
Author: Sophie M. Korn, Julian Von Ehr, Karthikeyan Dhamotharan, Jan-Niklas Tants, Rupert Abele and Andreas Schlundt
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