NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C
AUTOR(ES)
Inoue, Makoto
FONTE
Oxford University Press
RESUMO
Hu antigen C (HuC) has three RNA-binding domains (RBDs). The N-terminal two, RBD1 and RBD2, are linked in tandem and bind to the AU-rich elements (AREs) in the 3′-untranslated region of particular mRNAs. The solution structures of HuC RBD1 and RBD2 were determined by NMR methods. The HuC RBD1 and RBD2 structures are quite similar to those of Sxl RBD1 and RBD2, respectively. The individual RBDs of HuC, RBD1 and RBD2 in isolation can interact rather weakly with the minimal ARE motif, AUUUA, while the didomain fragment, RBD1–RBD2, of HuC binds more tightly to a longer ARE RNA, UAUUUAUUUU. Chemical shift perturbations by the longer RNA on HuC RBD1–RBD2 were mapped on and around the two β-sheets and on the C-terminal region of RBD1. The HuC RBD1–RBD2 residues that exhibited significant chemical shift perturbations coincide with those conserved in Sxl RBD1–RBD2. These data indicate that the RNA-binding characteristics of the HuC and Sxl didomain fragments are similar, even though the target RNAs and the biological functions of the proteins are different.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=102815Documentos Relacionados
- The Herpesvirus saimiri Small Nuclear RNAs Recruit AU-Rich Element-Binding Proteins but Do Not Alter Host AU-Rich Element-Containing mRNA Levels in Virally Transformed T Cells
- Functional characterization of a non-AUUUA AU-rich element from the c-jun proto-oncogene mRNA: evidence for a novel class of AU-rich elements.
- Two different RNA binding activities for the AU-rich element and the poly(A) sequence of the mouse neuronal protein mHuC.
- Highly Selective Actions of HuR in Antagonizing AU-Rich Element-Mediated mRNA Destabilization
- Purification, characterization, and cDNA cloning of an AU-rich element RNA-binding protein, AUF1.