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Conformational dynamics from ambiguous zinc coordination in the RanBP2-type zinc finger of RBM5.

J. Mol. Biol. 432, 4127-4138 (2020)
Postprint DOI Verlagsversion bestellen
Open Access Green
The multi-domain RNA binding protein RBM5 is a molecular signature of metastasis. RBM5 regulates alternative splicing of apoptotic genes including the cell death receptor Fas and the initiator Caspase-2. The RBM5 RanBP2-type zinc finger (Zf1) is known to specifically recognize single-stranded RNAs with high affinity. Here, we study the structure and conformational dynamics of the Zf1 zinc finger of human RBM5 using NMR. We show that the presence of a non-canonical cysteine in Zf1 kinetically destabilizes the protein. Metal-exchange kinetics show that mutation of the cysteine establishes high-affinity coordination of the zinc. Our data indicate that selection of such a structurally destabilizing mutation during the course of evolution could present an opportunity for functional adaptation of the protein.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Rbm5 ; Ranbp2 Zinc Finger ; Nmr; Candidate Tumor-suppressor; Cysteine Residues; Nmr-spectroscopy; P44 Subunit; Rna-binding; Protein; Domain; Recognition; Relaxation; Identification
ISSN (print) / ISBN 0022-2836
e-ISSN 1089-8638
Quellenangaben Band: 432, Heft: 14, Seiten: 4127-4138 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort 24-28 Oval Rd, London Nw1 7dx, England
Begutachtungsstatus Peer reviewed