The zinc fingers of the SR-like protein ZRANB2 are single-stranded RNA-binding domains that recognize 5' splice site-like sequences. Loughlin, F., Mansfield, R., Vaz, P., McGrath, A., Setiyaputra, S., Gamsjaeger, R., Chen, E., Morris, B., Guss, J., & Mackay, J. Proceedings of the National Academy of Sciences of the United States of America, 106(14):5581-5586, 2009. cited By 57
The zinc fingers of the SR-like protein ZRANB2 are single-stranded RNA-binding domains that recognize 5' splice site-like sequences [link]Paper  doi  abstract   bibtex   
The alternative splicing of mRNA is a critical process in higher eukaryotes that generates substantial proteomic diversity. Many of the proteins that are essential to this process contain arginine/serine-rich (RS) domains. ZRANB2 is a widely-expressed and highly-conserved RS-domain protein that can regulate alternative splicing but lacks canonical RNA-binding domains. Instead, it contains 2 RanBP2-type zinc finger (ZnF) domains. We demonstrate that these ZnFs recognize ssRNA with high affinity and specificity. Each ZnF binds to a single AGGUAA motif and the 2 domains combine to recognize AGGUAA (Nx) AGGUAA double sites, suggesting that ZRANB2 regulates alternative splicing via a direct interaction with pre-mRNA at sites that resemble the consensus 5' splice site. We show using X-ray crystallography that recognition of an AGGUAA motif by a single ZnF is dominated by side-chain hydrogen bonds to the bases and formation of a guanine-tryptophan-guanine ''ladder.'' A number of other human proteins that function in RNA processing also contain RanBP2 ZnFs in which the RNA-binding residues of ZRANB2 are conserved. The ZnFs of ZRANB2 therefore define another class of RNA-binding domain, advancing our understanding of RNA recognition and emphasizing the versatility of domains in molecular recognition.
@ARTICLE{Loughlin20095581,
author={Loughlin, F.E. and Mansfield, R.E. and Vaz, P.M. and McGrath, A.P. and Setiyaputra, S. and Gamsjaeger, R. and Chen, E.S. and Morris, B.J. and Guss, J.M. and Mackay, J.P.},
title={The zinc fingers of the SR-like protein ZRANB2 are single-stranded RNA-binding domains that recognize 5' splice site-like sequences},
journal={Proceedings of the National Academy of Sciences of the United States of America},
year={2009},
volume={106},
number={14},
pages={5581-5586},
doi={10.1073/pnas.0802466106},
note={cited By 57},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-65249133459&doi=10.1073%2fpnas.0802466106&partnerID=40&md5=698a9f6211fe20c6f2747b49bef7afc3},
affiliation={School of Molecular and Microbial Biosciences, School of Medical Sciences, University of Sydney, Sydney NSW 2006, Australia},
abstract={The alternative splicing of mRNA is a critical process in higher eukaryotes that generates substantial proteomic diversity. Many of the proteins that are essential to this process contain arginine/serine-rich (RS) domains. ZRANB2 is a widely-expressed and highly-conserved RS-domain protein that can regulate alternative splicing but lacks canonical RNA-binding domains. Instead, it contains 2 RanBP2-type zinc finger (ZnF) domains. We demonstrate that these ZnFs recognize ssRNA with high affinity and specificity. Each ZnF binds to a single AGGUAA motif and the 2 domains combine to recognize AGGUAA (Nx) AGGUAA double sites, suggesting that ZRANB2 regulates alternative splicing via a direct interaction with pre-mRNA at sites that resemble the consensus 5' splice site. We show using X-ray crystallography that recognition of an AGGUAA motif by a single ZnF is dominated by side-chain hydrogen bonds to the bases and formation of a guanine-tryptophan-guanine ''ladder.'' A number of other human proteins that function in RNA processing also contain RanBP2 ZnFs in which the RNA-binding residues of ZRANB2 are conserved. The ZnFs of ZRANB2 therefore define another class of RNA-binding domain, advancing our understanding of RNA recognition and emphasizing the versatility of domains in molecular recognition.},
author_keywords={Protein structure;  RanBP2 zinc fingers;  RNA-binding proteins;  Splicing},
keywords={adenine;  guanine;  protein zranb2;  single stranded RNA;  tryptophan;  unclassified drug;  zinc finger protein, alternative RNA splicing;  article;  hydrogen bond;  priority journal;  protein binding;  protein domain;  protein motif;  protein RNA binding;  protein structure;  RNA binding;  RNA processing;  X ray crystallography, Amino Acid Sequence;  Binding Sites;  Humans;  Protein Structure, Tertiary;  RNA;  RNA Splice Sites;  RNA-Binding Proteins;  Zinc Fingers, Eukaryota},
correspondence_address1={Mackay, J. P.; School of Molecular and Microbial Biosciences, , Sydney NSW 2006, Australia; email: j.mackay@usyd.edu.au},
issn={00278424},
coden={PNASA},
pubmed_id={19304800},
language={English},
abbrev_source_title={Proc. Natl. Acad. Sci. U. S. A.},
document_type={Article},
source={Scopus},
}
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