Nature Structural & Molecular Biology
- 11, 1054 - 1059 (2004)
Published online: 24 October 2004; Corrected online: 20 March 2007 | doi:10.1038/nsmb850
There is an Erratum (April 2007) associated with this Article.
Structural basis for the control of translation initiation during stressAntón Vila-Sanjurjo1, 2, 3, Barbara-S Schuwirth1, 2, 3, Cathy W Hau1, 2 & Jamie H D Cate1, 21
Departments of Molecular and Cell Biology and Chemistry, University of California, Berkeley, California
94720, USA. 2
Lawrence Berkeley National Laboratory, Physical Biosciences Division, Berkeley, California
94720, USA. 3
These authors contributed equally to this work.
Correspondence should be addressed to Jamie H D Cate jcate@lbl.gov During environmental stress, organisms limit protein synthesis by storing inactive ribosomes that are rapidly reactivated when conditions improve. Here we present structural and biochemical data showing that protein Y, an Escherichia coli stress protein, fills the tRNA- and mRNA-binding channel of the small ribosomal subunit to stabilize intact ribosomes. Protein Y inhibits translation initiation during cold shock but not at normal temperatures. Furthermore, protein Y competes with conserved translation initiation factors that, in bacteria, are required for ribosomal subunit dissociation. The mechanism used by protein Y to reduce translation initiation during stress and quickly release ribosomes for renewed translation initiation may therefore occur widely in nature.
MORE ARTICLES LIKE THIS These links to content published by NPG are automatically generated.
|
