NDLI: Backbone resonance assignments of the m1A22 tRNA methyltransferase TrmK from Bacillus subtilis

Content Provider	Springer Nature Link
Author	Dégut, Clément Barraud, Pierre Larue, Valéry Tisné, Carine
Copyright Year	2016
Abstract	RNA modification is a post-transcriptional process by which certain nucleotides are altered after their initial incorporation into an RNA chain. Transfer RNAs (tRNAs) is the most heavily modified class of RNA molecules. These modifications expand the chemical and functional diversity of tRNAs and enhance their structural stability. To date, more than 100 modifications have been identified, the majority of which are specific from one domain of life. However, few modifications are extensively present in the three domains of life. Among those, the m$^{1}$A nucleotide, which consists in the methylation at position 1 of the adenine aromatic ring, is found in tRNAs and ribosomal RNAs. In tRNAs, the m$^{1}$A modification occurs at position 9, 14, 22, 57 and 58. The enzyme TrmK catalyzes the m$^{1}$A formation at position 22. Here we report the backbone $^{1}$H, $^{15}$N and $^{13}$C chemical shift assignments of TrmK from Bacillus subtilis obtained by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution as predicted by TALOS+. These assignments of TrmK pave the way for interaction studies with its tRNA substrates.
Starting Page	253
Ending Page	257
Page Count	5
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	10
Issue Number	2
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2016-04-20
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Backbone resonance assignment Heteronuclear NMR Unlabeling Methyltransferase TrmK tRNA m$^{1}$A Biophysics and Biological Physics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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