Summary information and primary citation
- PDB-id
-
5m0j;
DSSR-derived features in text and
JSON formats
- Class
- RNA binding protein
- Method
- X-ray (2.8 Å)
- Summary
- Crystal structure of the cytoplasmic complex with
she2p, she3p, and the ash1 mrna e3-localization
element
- Reference
-
Edelmann FT, Schlundt A, Heym RG, Jenner A,
Niedner-Boblenz A, Syed MI, Paillart JC, Stehle R,
Janowski R, Sattler M, Jansen RP, Niessing D (2017):
"Molecular
architecture and dynamics of ASH1 mRNA recognition by its
mRNA-transport complex." Nat. Struct. Mol.
Biol., 24, 152-161. doi: 10.1038/nsmb.3351.
- Abstract
- mRNA localization is an essential mechanism of gene
regulation and is required for processes such as stem-cell
division, embryogenesis and neuronal plasticity. It is not
known which features in the cis-acting mRNA localization
elements (LEs) are specifically recognized by
motor-containing transport complexes. To the best of our
knowledge, no high-resolution structure is available for
any LE in complex with its cognate protein complex. Using
X-ray crystallography and complementary techniques, we
carried out a detailed assessment of an LE of the ASH1 mRNA
from yeast, its complex with its shuttling RNA-binding
protein She2p, and its highly specific, cytoplasmic complex
with She3p. Although the RNA alone formed a flexible stem
loop, She2p binding induced marked conformational changes.
However, only joining by the unstructured She3p resulted in
specific RNA recognition. The notable RNA rearrangements
and joint action of a globular and an unfolded RNA-binding
protein offer unprecedented insights into the step-wise
maturation of an mRNA-transport complex.
