Backbone resonance assignments of the 48 kDa dimeric putative 18S rRNA-methyltransferase Nep1 from Methanocaldococcus jannaschii

Biomol NMR Assign. 2009 Dec;3(2):251-4. doi: 10.1007/s12104-009-9187-z.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Methanococcales / enzymology*
  • Methyltransferases / chemistry*
  • Methyltransferases / metabolism*
  • Models, Molecular
  • Molecular Weight
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Multimerization*
  • Protein Structure, Quaternary
  • RNA, Ribosomal, 18S / metabolism*


  • RNA, Ribosomal, 18S
  • Methyltransferases