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Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase.
- L. Frolova, X. Le Goff, G. Zhouravleva, E. Davydova, M. Philippe, L. Kisselev
- Biology, MedicineRNA
- 1 April 1996
It is demonstrated that eRF3 is a GTP-binding protein endowed with a negligible, if any, intrinsic GTPase activity that is profoundly stimulated by the joint action of eRF1 and the ribosome, and that in ribosomes both hydrolytic reactions are mediated by the formation of the ternary eRF-eRF3-GTP complex.
Lysine methylation of VCP by a member of a novel human protein methyltransferase family.
- S. Kernstock, E. Davydova, +5 authors P. Falnes
- Biology, MedicineNature communications
- 4 September 2012
It is shown that mammalian VCP is trimethylated on Lys315 in a variety of cell lines and tissues, and that the previously uncharacterized protein METTL21D (denoted here as VCP lysine methyltransferase, VCP-KMT) is the responsible enzyme.
Protein lysine methylation by seven-β-strand methyltransferases.
- P. Falnes, Magnus E. Jakobsson, E. Davydova, A. Ho, J. Małecki
- Biology, MedicineThe Biochemical journal
- 15 July 2016
A number of novel 7BS KMTs have now been discovered, and, in particular, several recently characterized human and yeast members of MTase family 16 (MTF16) have been found to methylate lysines in non-histone proteins.
Identification and Characterization of a Novel Evolutionarily Conserved Lysine-specific Methyltransferase Targeting Eukaryotic Translation Elongation Factor 2 (eEF2)*
- E. Davydova, A. Ho, +5 authors P. Falnes
- Biology, MedicineThe Journal of Biological Chemistry
- 17 September 2014
The present study establishes the function of the previously uncharacterized MTases FAM86A and Yjr129c, demonstrating that these enzymes introduce a functionally important lysine methylation in eEF2.
Light Signaling Mechanism of Two Tandem Bacteriophytochromes.
- Xiaojing Yang, E. Stojković, W. B. Ozarowski, J. Kuk, E. Davydova, K. Moffat
- Biology, MedicineStructure
- 7 July 2015
These structures, together with mutational studies, provide insights into photoconversion and the long-range signaling mechanism in phytochromes.
Saccharomyces cerevisiae Eukaryotic Elongation Factor 1A (eEF1A) Is Methylated at Lys-390 by a METTL21-Like Methyltransferase
- Magnus E. Jakobsson, E. Davydova, J. Małecki, A. Moen, P. Falnes
- Biology, MedicinePloS one
- 26 June 2015
The results demonstrate that Ynl024c is the enzyme responsible for methylation of eEF1A at Lys390, and in accordance with prior naming of similar enzymes, the YNL024c protein is suggested to be renamed to Efm6 (Elongation factor MTase 6).
The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes
It is reported that METTL9 is a broad-specificity methyltransferase that mediates the formation of the majority of 1MH present in mouse and human proteomes, and the results establishMETTL9-mediated 1MH as a pervasive protein modification, thus setting the stage for further functional studies on protein histidine methylation.
Human METTL18 is a histidine-specific methyltransferase that targets RPL3 and affects ribosome biogenesis and function
- J. Małecki, Marie-Francoise Odonohue, +11 authors P. Falnes
- MedicineNucleic acids research
- 8 March 2021
METTL18 is established as the second human histidine-specific protein MTase, and its functional relevance is demonstrated, indicating that METTL18-mediated methylation of RPL3 is important for optimal ribosome biogenesis and function.
Protozoan ALKBH8 Oxygenases Display both DNA Repair and tRNA Modification Activities
All the enzymes showed DNA repair activity in vitro, but, interestingly, two protozoan ALKBH8s also catalyzed wobble uridine modification of tRNA, thus displaying a dual in vitro activity.
The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates
- Magnus E. Jakobsson, J. Małecki, +11 authors P. Falnes
- Chemistry, MedicineNature Communications
- 24 August 2018
The authors identify METTL13 as an eEF1A methyltransferase with dual specificity, which is involved in the codon-specific modulation of mRNA translation.