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Author Notes:

To whom correspondence should be addressed at: Department of Biochemistry, Emory University School of Medicine, 1510 Clifton Road NE, RRC Room 4117, Atlanta, GA 30322-2430. E-mail: acorbe2@emory.edu

Edited by Aaron Klug, Medical Research Council, Cambridge, United Kingdom, and approved June 14, 2007

Author contributions: S.M.K. and S.A.P. contributed equally to this work; S.M.K., S.A.P., C.M.K., A.H.C., and K.M.B. designed research; S.M.K., S.A.P., and P.G. performed research; S.M.K., S.A.P., and K.A.M. contributed new reagents/analytic tools; S.M.K., S.A.P., C.M.K., P.G., T.J.M., A.H.C., and K.M.B. analyzed data; and S.M.K., S.A.P., A.H.C., and K.M.B. wrote the paper.


Research Funding:

This work was supported by grants from the National Institutes of Health (to A.H.C. and K.M.B.).


  • CCCH zinc finger
  • poly(A) binding protein
  • RNA binding

Recognition of polyadenosine RNA by zinc finger proteins


Journal Title:

Proceedings of the National Academy of Sciences


Volume 104, Number 30


, Pages 12306-12311

Type of Work:

Article | Post-print: After Peer Review


Messenger RNA transcripts are coated from cap to tail with a dynamic combination of RNA binding proteins that process, package, and ultimately regulate the fate of mature transcripts. One class of RNA binding proteins essential for multiple aspects of mRNA metabolism consists of the poly(A) binding proteins. Previous studies have concentrated on the canonical RNA recognition motif-containing poly(A) binding proteins as the sole family of poly(A)-specific RNA binding proteins. In this study, we present evidence for a previously uncharacterized poly(A) recognition motif consisting of tandem CCCH zinc fingers. We have probed the nucleic acid binding properties of a yeast protein, Nab2, that contains this zinc finger motif. Results of this study reveal that the seven tandem CCCH zinc fingers of Nab2 specifically bind to polyadenosine RNA with high affinity. Furthermore, we demonstrate that a human protein, ZC3H14, which contains CCCH zinc fingers homologous to those found in Nab2, also specifically binds polyadenosine RNA. Thus, we propose that these proteins are members of an evolutionarily conserved family of poly(A) RNA binding proteins that recognize poly(A) RNA through a fundamentally different mechanism than previously characterized RNA recognition motif-containing poly(A) binding proteins.

Copyright information:

© 2007 by The National Academy of Sciences of the USA

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