Panvert, Michel and Dubiez, Etienne and Arnold, Lea and Perez, Javier and Mechulam, Yves and Seufert, Wolfgang and Schmitt, Emmanuelle (2015) Cdc123, a Cell Cycle Regulator Needed for eIF2 Assembly, Is an ATP-Grasp Protein with Unique Features. STRUCTURE, 23 (9). pp. 1596-1608. ISSN 0969-2126, 1878-4186
Full text not available from this repository. (Request a copy)Abstract
Eukaryotic initiation factor 2 (eIF2), a heterotrimeric guanosine triphosphatase, has a central role in protein biosynthesis by supplying methionylated initiator tRNA to the ribosomal translation initiation complex and by serving as a target for translational control in response to stress. Recent work identified a novel step indispensable for eIF2 function: assembly of eIF2 from its three subunits by the cell proliferation protein Cdc123. We report the first crystal structure of a Cdc123 representative, that from Schizosaccharomyces pombe, both isolated and bound to domain III of Saccharomyces cerevisiae eIF2 gamma. The structures show that Cdc123 resembles enzymes of the ATP-grasp family. Indeed, Cdc123 binds ATP-Mg2+, and conserved residues contacting ATP-Mg2+ are essential for Cdc123 to support eIF2 assembly and cell viability. A docking of eIF2 alpha gamma onto Cdc123, combined with genetic and biochemical experiments, allows us to propose a model explaining how Cdc123 participates in the biogenesis of eIF2 through facilitating assembly of eIF2 gamma to eIF2 alpha.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TRANSLATION INITIATION-FACTOR; START-SITE SELECTION; CRYSTAL-STRUCTURE; TRANSFER-RNA; SACCHAROMYCES-CEREVISIAE; BIOTIN CARBOXYLASE; GTP HYDROLYSIS; LINE 3Y1; LIGASE; COMPLEX; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 12 Jun 2019 13:30 |
| Last Modified: | 12 Jun 2019 13:30 |
| URI: | https://pred.uni-regensburg.de/id/eprint/4924 |
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