TRNA:m2G6 methyltransferase TrmN/Trm14
From Proteopedia
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| + | == Introduction == | ||
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TrmN and Trm14 build a family of tRNA:m2G6 methylstransferases, that specifically modify a guanosine on position 6 of tRNA. Transfer RNA (tRNA) molecules are pivotal in the translation of the genetic code into protein sequence. tRNAs consist of 54 to 100 nucleotides (mostly 76 nucleotides) and form a 3-dimensional L-shaped structure and more than 100 tRNA modifications are known up to date, where methylations are the most common ones. Modifications of tRNA can affect the tRNA conformation and thereby also the base pairing capabilities of the anticodon, base pairing with the mRNA codon due to modifications at the anticodon and the recognition by aminoacyl tRNA synthetases at the acceptor stem. Although many tRNA modifications are known, often the proteins involved in the modification are unknown. | TrmN and Trm14 build a family of tRNA:m2G6 methylstransferases, that specifically modify a guanosine on position 6 of tRNA. Transfer RNA (tRNA) molecules are pivotal in the translation of the genetic code into protein sequence. tRNAs consist of 54 to 100 nucleotides (mostly 76 nucleotides) and form a 3-dimensional L-shaped structure and more than 100 tRNA modifications are known up to date, where methylations are the most common ones. Modifications of tRNA can affect the tRNA conformation and thereby also the base pairing capabilities of the anticodon, base pairing with the mRNA codon due to modifications at the anticodon and the recognition by aminoacyl tRNA synthetases at the acceptor stem. Although many tRNA modifications are known, often the proteins involved in the modification are unknown. | ||
| - | In 2011 Menenez et al. (1) identified in the archeum M. jannaschii an enzyme called Trm14 which is responsible for the m2G modification of tRNA(Cys). Independendly Roovers et al. (2) identified the orthologous protein TrmN in the bacterium Thermus thermophilus, which is capable of modifying tRNA(Phe). | + | In 2011 Menenez ''et al''. (1) identified in the archeum ''M. jannaschii'' an enzyme called Trm14 which is responsible for the m2G modification of tRNA(Cys). Independendly Roovers ''et al''. (2) identified the orthologous protein TrmN in the bacterium Thermus thermophilus, which is capable of modifying tRNA(Phe). |
| + | == Structures == | ||
| + | For this family four structures are existing of which one [[3tma]] is the crystal structure of TrmN from the bacterium ''Thermus thermophilus'' and three [[3tlj]], [[3tl4]] and [[3tm5]] are the crystal structures of Trm14 from the archaeum ''Pyrococcus furiosus''. Additionally this protein exist also in eukaryotes but their structure is missing. | ||
| + | == References == | ||
| - | (1)Menezes S, Gaston KW, Krivos KL, Apolinario EE, Reich NO, Sowers KR, Limbach PA, Perona JJ., Nucleic Acids Res. 2011 Sep 1;39(17):7641-55. Epub 2011 Jun 21, Formation of m2G6 in Methanocaldococcus jannaschii tRNA catalyzed by the novel methyltransferase Trm14 | + | (1) Menezes S, Gaston KW, Krivos KL, Apolinario EE, Reich NO, Sowers KR, Limbach PA, Perona JJ., Nucleic Acids Res. 2011 Sep 1;39(17):7641-55. Epub 2011 Jun 21, Formation of m2G6 in Methanocaldococcus jannaschii tRNA catalyzed by the novel methyltransferase Trm14 |
(2) Roovers M, Oudjama Y, Fislage M, Bujnicki JM, Versées W, Droogmans L., RNA. 2012 Apr;18(4):815-24. Epub 2012 Feb 15., The open reading frame TTC1157 of Thermus thermophilus HB27 encodes the methyltransferase forming N²-methylguanosine at position 6 in tRNA. | (2) Roovers M, Oudjama Y, Fislage M, Bujnicki JM, Versées W, Droogmans L., RNA. 2012 Apr;18(4):815-24. Epub 2012 Feb 15., The open reading frame TTC1157 of Thermus thermophilus HB27 encodes the methyltransferase forming N²-methylguanosine at position 6 in tRNA. | ||
Revision as of 12:51, 8 June 2012
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Introduction
TrmN and Trm14 build a family of tRNA:m2G6 methylstransferases, that specifically modify a guanosine on position 6 of tRNA. Transfer RNA (tRNA) molecules are pivotal in the translation of the genetic code into protein sequence. tRNAs consist of 54 to 100 nucleotides (mostly 76 nucleotides) and form a 3-dimensional L-shaped structure and more than 100 tRNA modifications are known up to date, where methylations are the most common ones. Modifications of tRNA can affect the tRNA conformation and thereby also the base pairing capabilities of the anticodon, base pairing with the mRNA codon due to modifications at the anticodon and the recognition by aminoacyl tRNA synthetases at the acceptor stem. Although many tRNA modifications are known, often the proteins involved in the modification are unknown. In 2011 Menenez et al. (1) identified in the archeum M. jannaschii an enzyme called Trm14 which is responsible for the m2G modification of tRNA(Cys). Independendly Roovers et al. (2) identified the orthologous protein TrmN in the bacterium Thermus thermophilus, which is capable of modifying tRNA(Phe).
Structures
For this family four structures are existing of which one 3tma is the crystal structure of TrmN from the bacterium Thermus thermophilus and three 3tlj, 3tl4 and 3tm5 are the crystal structures of Trm14 from the archaeum Pyrococcus furiosus. Additionally this protein exist also in eukaryotes but their structure is missing.
References
(1) Menezes S, Gaston KW, Krivos KL, Apolinario EE, Reich NO, Sowers KR, Limbach PA, Perona JJ., Nucleic Acids Res. 2011 Sep 1;39(17):7641-55. Epub 2011 Jun 21, Formation of m2G6 in Methanocaldococcus jannaschii tRNA catalyzed by the novel methyltransferase Trm14 (2) Roovers M, Oudjama Y, Fislage M, Bujnicki JM, Versées W, Droogmans L., RNA. 2012 Apr;18(4):815-24. Epub 2012 Feb 15., The open reading frame TTC1157 of Thermus thermophilus HB27 encodes the methyltransferase forming N²-methylguanosine at position 6 in tRNA.
