Trm112p Is a 15-kDa Zinc Finger Protein Essential for the Activity of Two tRNA and One Protein Methyltransferases in Yeast

Autor: Léon Dirick, Bruno Lapeyre, Glenn R. Björk, Marie-Hélène Mazauric, Suresh K. Purushothaman
Přispěvatelé: Centre de recherches de biochimie macromoléculaire ( CRBM ), Université Montpellier 1 ( UM1 ) -Université Montpellier 2 - Sciences et Techniques ( UM2 ) -IFR122-Centre National de la Recherche Scientifique ( CNRS ), Institut de Génétique Moléculaire de Montpellier ( IGMM ), Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Centre de recherche en Biologie Cellulaire (CRBM), Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1), Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)
Rok vydání: 2010
Předmět:
Proteomics
MESH : DNA
MESH: tRNA Methyltransferases
MESH : Saccharomyces cerevisiae
MESH : Models
Genetic
Biochemistry
MESH: Recombinant Proteins
MESH : Proteomics
MESH: Saccharomyces cerevisiae Proteins
MESH : Anticodon
RNA
Transfer
MESH : Catalysis
MESH: Models
Genetic
Zinc finger
tRNA Methyltransferases
MESH : Cell Nucleus
0303 health sciences
MESH : Chromatin
MESH: Proteomics
030302 biochemistry & molecular biology
MESH: DNA
Zinc Fingers
MESH : Protein Binding
Translation (biology)
MESH: Saccharomyces cerevisiae
MESH : Mitosis
Chromatin
Recombinant Proteins
MESH : tRNA Methyltransferases
Transfer RNA
T arm
MESH : Mutation
Protein Binding
MESH: Cell Nucleus
TRNA modification
Saccharomyces cerevisiae Proteins
MESH: Mutation
MESH : Recombinant Proteins
Saccharomyces cerevisiae
Mitosis
MESH : RNA
Transfer
Biology
Catalysis
Chromatin remodeling
MESH: Chromatin
MESH : Saccharomyces cerevisiae Proteins
03 medical and health sciences
Anticodon
MESH: Anticodon
MESH: Zinc Fingers
MESH: Protein Binding
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
MESH : Zinc Fingers
[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry
Molecular Biology
Molecular Biology
030304 developmental biology
Cell Nucleus
Models
Genetic
TRNA Methyltransferase
DNA
Cell Biology
MESH: Mitosis
MESH: Catalysis
MESH: RNA
Transfer
biology.organism_classification
Mutation
RNA
Zdroj: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2010, 285 (24), pp.18505-15. 〈10.1074/jbc.M110.113100〉
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2010, 285 (24), pp.18505-18515. ⟨10.1074/jbc.M110.113100⟩
ISSN: 0021-9258
1083-351X
DOI: 10.1074/jbc.m110.113100
Popis: International audience; The degenerate base at position 34 of the tRNA anticodon is the target of numerous modification enzymes. In Saccharomyces cerevisiae, five tRNAs exhibit a complex modification of uridine 34 (mcm(5)U(34) and mcm(5)s(2)U(34)), the formation of which requires at least 25 different proteins. The addition of the last methyl group is catalyzed by the methyltransferase Trm9p. Trm9p interacts with Trm112p, a 15-kDa protein with a zinc finger domain. Trm112p is essential for the activity of Trm11p, another tRNA methyltransferase, and for Mtq2p, an enzyme that methylates the translation termination factor eRF1/Sup45. Here, we report that Trm112p is required in vivo for the formation of mcm(5)U(34) and mcm(5)s(2)U(34). When produced in Escherichia coli, Trm112p forms a complex with Trm9p, which renders the latter soluble. This recombinant complex catalyzes the formation of mcm(5)U(34) on tRNA in vitro but not mcm(5)s(2)U(34). An mtq2-0 trm9-0 strain exhibits a synthetic growth defect, thus revealing the existence of an unexpected link between tRNA anticodon modification and termination of translation. Trm112p is associated with other partners involved in ribosome biogenesis and chromatin remodeling, suggesting that it has additional roles in the cell.
Databáze: OpenAIRE
Externí odkaz: