English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

The bicoid mRNA localization factor Exuperantia is an RNA-binding pseudonuclease.

MPS-Authors
/persons/resource/persons36541

Kramer,  K.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15947

Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)

2332063_Suppl_1.html
(Supplementary material), 77KB

2332063_Suppl_2.html
(Supplementary material), 75KB

2332063_Suppl_3.html
(Supplementary material), 76KB

2332063_Suppl_4.html
(Supplementary material), 75KB

2332063_Suppl_5.html
(Supplementary material), 76KB

2332063_Suppl_6.html
(Supplementary material), 75KB

2332063_Suppl_7.html
(Supplementary material), 76KB

2332063_Suppl_8.pdf
(Supplementary material), 3MB

2332063_Suppl_9.pdf
(Supplementary material), 4MB

2332063_Suppl_10.xlsx
(Supplementary material), 26KB

Citation

Lazzaretti, D., Veith, K., Kramer, K., Basquin, C., Urlaub, H., Iron, U., et al. (2016). The bicoid mRNA localization factor Exuperantia is an RNA-binding pseudonuclease. Nature Structural and Molecular Biology, 23(8), 705-713. doi:10.1038/nsmb.3254.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-2F22-C
Abstract
Anterior patterning in Drosophila is mediated by the localization of bicoid (bcd) mRNA at the anterior pole of the oocyte. Exuperantia (Exu) is a putative exonuclease (EXO) associated with bcd and required for its localization. We present the crystal structure of Exu, which reveals a dimeric assembly with each monomer consisting of a 3′-5′ EXO-like domain and a sterile alpha motif (SAM)-like domain. The catalytic site is degenerate and inactive. Instead, the EXO-like domain mediates dimerization and RNA binding. We show that Exu binds RNA directly in vitro, that the SAM-like domain is required for RNA binding activity and that Exu binds a structured element present in the bcd 3′ untranslated region with high affinity. Through structure-guided mutagenesis, we show that Exu dimerization is essential for bcd localization. Our data demonstrate that Exu is a noncanonical RNA-binding protein with EXO-SAM-like domain architecture that interacts with its target RNA as a homodimer.