TY  - JOUR
A1  - Korn, Sophie M.
A1  - Ehr, Julian von
A1  - Dhamotharan, Karthikeyan
A1  - Tants, Jan-Niklas
A1  - Abele, Rupert
A1  - Schlundt, Andreas
T1  - Insight into the structural basis for dual nucleic acid - recognition by the Scaffold Attachment Factor B2 protein
T2  - International Journal of Molecular Sciences
N2  - 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.
KW  - scaffold attachment factor proteins
KW  - nuclear matrix
KW  - nuclear magnetic resonance spectroscopy
KW  - SAP domain
KW  - RRM domain
KW  - dual nucleic acid binding
KW  - chromatin
KW  - RNA processing
KW  - protein dynamics
Y1  - 2023
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/75116
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-751160
SN  - 1422-0067
VL  - 24
IS  - 4, art. 3286
PB  - MDPI
CY  - Basel
ER  -