Molecular recognition of an RNA trafficking element by heterogeneous nuclear ribonucleoprotein A2

Landsberg, Michael J., Moran-Jones, Kim and Smith, Ross (2006) Molecular recognition of an RNA trafficking element by heterogeneous nuclear ribonucleoprotein A2. Biochemistry, 45 12: 3943-3951. doi:10.1021/bi052440e

Author Landsberg, Michael J.
Moran-Jones, Kim
Smith, Ross
Title Molecular recognition of an RNA trafficking element by heterogeneous nuclear ribonucleoprotein A2
Journal name Biochemistry   Check publisher's open access policy
ISSN 0006-2960
Publication date 2006
Sub-type Article (original research)
DOI 10.1021/bi052440e
Volume 45
Issue 12
Start page 3943
End page 3951
Total pages 9
Place of publication Washington D.C., USA
Publisher American Chemical Society
Collection year 2006
Language eng
Subject C1
270199 Biochemistry and Cell Biology not elsewhere classified
780105 Biological sciences
Abstract Heterogeneous nuclear ribonucleoprotein (hnRNP) A2 is a multitasking protein involved in RNA packaging, alternative splicing of pre-mRNA. telomere maintenance, cytoplasmic RNA trafficking, and translation. It binds short segments of single-stranded nucleic acids, including the A2RE11 RNA element that is necessary and sufficient for cytoplasmic transport of a subset of rnRNAs in oligodendrocytes and neurons. We have explored the structures of hnRNP A2, its RNA recognition motifs (RRMs) and Gly-rich module, and the RRM complexes with A2RE11. Circular dichroism spectroscopy showed that the secondary structure of the first 189 residues of hnRNP A2 parallels that of the tandem beta alpha beta beta alpha beta RRMs of its paralogue, hnRNP A1, previously deduced from X-ray diffraction studies. The unusual GRD was shown to have substantial beta-sheet and beta-turn structure. Sedimentation equilibrium and circular dichroism results were consistent with the tandem RRM region being monomeric and supported earlier evidence for the binding of two A2RE11 oligoribonucleotides to this domain, in contrast to the protein dimer formed by the complex of hnRNP A1 with the telomeric ssDNA repeat. A three-dimensional structure for the N-terminal, two-RRM-containing segment of hnRNP A2 was derived by homology modeling. This structure was used to derive a model for the complex with A2RE11 using the previously described interaction of pairs of stacked nucleotides with aromatic residues on the RRM beta-sheet platforms, conserved in other RRM-RNA complexes, together with biochemical data and molecular dynamics-based observations of inter-RRM mobility.
Keyword Biochemistry & Molecular Biology
Protein Messenger-rna
Au-rich Element
Hnrnp A2
Response Element
Binding Domain
Secondary Structure
Q-Index Code C1

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Created: Wed, 15 Aug 2007, 09:00:02 EST