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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)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Rbm5 ; Ranbp2 Zinc Finger ; Nmr; Candidate Tumor-suppressor; Cysteine Residues; Nmr-spectroscopy; P44 Subunit; Rna-binding; Protein; Domain; Recognition; Relaxation; Identification
Language
english
Publication Year
2020
HGF-reported in Year
2020
ISSN (print) / ISBN
0022-2836
e-ISSN
1089-8638
Journal
Journal of Molecular Biology
Quellenangaben
Volume: 432,
Issue: 14,
Pages: 4127-4138
Publisher
Elsevier
Publishing Place
24-28 Oval Rd, London Nw1 7dx, England
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Enabling and Novel Technologies
PSP Element(s)
G-503000-001
WOS ID
WOS:000543017000012
Scopus ID
85085705653
PubMed ID
32450081
Erfassungsdatum
2020-06-17