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  Insight into the Structural Basis for Dual Nucleic Acid-Recognition by the Scaffold Attachment Factor B2 Protein

Korn, S. M., Ehr, J. v., Dhamotharan, K., Tants, J.-N., Abele, R., & Schlundt, A. (2023). Insight into the Structural Basis for Dual Nucleic Acid-Recognition by the Scaffold Attachment Factor B2 Protein. International Journal of Molecular Sciences, 24(4): 3286. doi:10.3390/ijms24043286.

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 Creators:
Korn, Sophie M.1, Author
Ehr, Julian von1, 2, Author                 
Dhamotharan, Karthikeyan1, Author
Tants, Jan-Niklas1, Author
Abele, Rupert3, Author
Schlundt, Andreas1, Author
Affiliations:
1Institute for Molecular Biosciences, Biomolecular Resonance Center (BMRZ), Goethe University Frankfurt, Frankfurt, Germany, ou_persistent22              
2IMPRS-CBP, Max Planck Institute of Biophysics, Max Planck Society, ou_3562496              
3Institute for Biochemistry, Goethe University Frankfurt, Frankfurt, Germany, ou_persistent22              

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Free keywords: chromatin, dual nucleic acid binding, nuclear magnetic resonance spectroscopy, nuclear matrix, protein dynamics, RNA processing, RRM domain, SAP domain, scaffold attachment factor proteins
 Abstract: 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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Language(s): eng - English
 Dates: 2023-01-302022-12-282023-02-032023-02-07
 Publication Status: Published online
 Pages: 22
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.3390/ijms24043286
BibTex Citekey: korn_insight_2023
 Degree: -

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Title: International Journal of Molecular Sciences
  Abbreviation : Int. J. Mol. Sci.
Source Genre: Journal
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Publ. Info: Basel, Switzerland : MDPI AG
Pages: - Volume / Issue: 24 (4) Sequence Number: 3286 Start / End Page: - Identifier: ISSN: 1422-0067
CoNE: https://pure.mpg.de/cone/journals/resource/1422-0067