期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 23, 页码 10406-10411出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1005389107
关键词
mRNA export machinery; fluorescence localization; microscopy; site-directed mutagenesis; protein-protein interaction
资金
- Leukemia and Lymphoma Society
The export of mRNAs is a multistep process, involving the packaging of mRNAs into messenger ribonucleoprotein particles (mRNPs), their transport through nuclear pore complexes, and mRNP remodeling events prior to translation. Ribonucleic acid export 1 (Rae1) and Nup98 are evolutionarily conserved mRNA export factors that are targeted by the vesicular stomatitis virus matrix protein to inhibit host cell nuclear export. Here, we present the crystal structure of human Rae1 in complex with the Gle2-binding sequence ( GLEBS) of Nup98 at 1.65 angstrom resolution. Rae1 forms a seven- bladed beta-propeller with several extensive surface loops. The Nup98 GLEBS motif forms an approximate to 50-angstrom-long hairpin that binds with its C-terminal arm to an essentially invariant hydrophobic surface that extends over the entire top face of the Rae1 beta-propeller. The C- terminal arm of the GLEBS hairpin is necessary and sufficient for Rae1 binding, and we identify a tandem glutamate element in this arm as critical for complex formation. The Rae1.Nup98(GLEBS) surface features an additional conserved patch with a positive electrostatic potential, and we demonstrate that the complex possesses single-stranded RNA-binding. capability. Together, these data suggest that the Rae1.Nup98 complex directly binds to the mRNP at several stages of the mRNA export pathway.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据