Does Glutamine Methylation Affect the Intrinsic Conformation of the Universally Conserved GGQ Motif in Ribosomal Release Factors?
Author:
Affiliation:
1. Department of Cell and Molecular Biology, Uppsala University, Biomedical Center, Box 596, SE-751 24 Uppsala, Sweden
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi900117r
Reference40 articles.
1. Polypeptide chain termination in vitro: isolation of a release factor.
2. The termination of translation
3. A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor
4. Characterization of reticulocyte release factor.
5. Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
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2. Bridging the gap between ribosome structure and biochemistry by mechanistic computations;Current Opinion in Structural Biology;2012-12
3. The Mechanism of Peptidyl Transfer Catalysis by the Ribosome;Annual Review of Biochemistry;2011-07-07
4. Mechanism of activation of methyltransferases involved in translation by the Trm112 ‘hub’ protein;Nucleic Acids Research;2011-04-07
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