UNIGE document Scientific Article
previous document  unige:24406  next document
add to browser collection
Title

Functional implications from the Cid1 poly(U) polymerase crystal structure

Authors
Published in Structure. 2012, vol. 20, no. 6, p. 977-86
Abstract In eukaryotes, mRNA degradation begins with poly(A) tail removal, followed by decapping, and the mRNA body is degraded by exonucleases. In recent years, the major influence of 3'-end uridylation as a regulatory step within several RNA degradation pathways has generated significant attention toward the responsible enzymes, which are called poly(U) polymerases (PUPs). We determined the atomic structure of the Cid1 protein, the founding member of the PUP family, in its UTP-bound form, allowing unambiguous positioning of the UTP molecule. Our data also suggest that the RNA substrate accommodation and product translocation by the Cid1 protein rely on local and global movements of the enzyme. Supplemented by point mutations, the atomic model is used to propose a catalytic cycle. Our study underlines the Cid1 RNA binding properties, a feature with critical implications for miRNAs, histone mRNAs, and, more generally, cellular RNA degradation.
Keywords Amino Acid MotifsAmino Acid SequenceCatalytic DomainConserved SequenceCrystallography, X-RayHydrogen BondingModels, MolecularMolecular Sequence DataNucleotidyltransferases/chemistryProtein BindingRNA, Fungal/chemistrySchizosaccharomyces/enzymologySchizosaccharomyces pombe Proteins/chemistrySubstrate SpecificitySurface PropertiesUridine Triphosphate/chemistry
Identifiers
PMID: 22608966
Full text
Structures
Projects FNS: 31003A-124909
FNS: 31003A-140924
Citation
(ISO format)
MUNOZ TELLO, Paola Andrea, GABUS-DARLIX, Caroline, THORE, Stéphane. Functional implications from the Cid1 poly(U) polymerase crystal structure. In: Structure, 2012, vol. 20, n° 6, p. 977-86. https://archive-ouverte.unige.ch/unige:24406

211 hits

0 download

Update

Deposited on : 2012-12-11

Export document
Format :
Citation style :