Backbone resonance assignments of the 48 kDa dimeric putative 18S rRNA-methyltransferase Nep1 from Methanocaldococcus jannaschii
- 138 Downloads
Nep1 from Methanocaldococcus jannaschii is a 48 kDa dimeric protein belonging to the SPOUT-class of S-adenosylmethionine dependent RNA-methyltransferases and acting as a ribosome assembly factor. Mutations in the human homolog are the cause of Bowen-Conradi syndrome. We report here 1H, 15N and 13C chemical shift assignments for the backbone of the protein in its apo state.
KeywordsNMR-assignments Triple resonance experiments RNA-methyltransferase SPOUT-class Nep1 Bowen-Conradi syndrome
We are grateful to Drs. Andrew P. Hinck and Christian Richter for helpful discussions. This project was supported by start-up funds from the Department of Biochemistry, University of Texas Health Science Center San Antonio (to J.W.), an Aventis Foundation Professorship (to J.W.), the Center of Biomolecular Magnetic Resonance, Johann-Wolfgang-Goethe-University Frankfurt, and the Deutsche Forschungsgemeinschaft (DFG) through the SFB 579 ‘RNA-Ligand Interactions’ (to J.W. and K.-D.E.). The Center of Biomolecular NMR Spectroscopy at UTHSCSA is supported by NIH Grants RR13879 and CA54174.
- Armistead J, Khatkar S, Meyer B, Mark BL, Patel N, Coghlan G, Lamont RE, Liu S, Wiechert J, Cattini PA, Koetter P, Wrogemann K, Greenberg CR, Entian KD, Zelinski T, Triggs-Raine B (2009) Mutation of a gene essential for ribosome biogenesis, EMG1, causes Bowen-Conradi syndrome. Am J Hum Genet 84:728–739CrossRefGoogle Scholar
- Keller R (2004) The computer aided resonance assignment tutorial. CANTINA Verlag, GoldauGoogle Scholar