Solution structure of the Vts1 SAM domain in the presence of RNA

Thomas A. Edwards, Joel A. Butterwick, Lei Zeng, Yogesh K. Gupta, Xin Wang, Robin P. Wharton, Arthur G. Palmer, Aneel K. Aggarwal

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


The yeast Vts1 SAM (sterile alpha motif) domain is a member of a new class of SAM domains that specifically bind RNA. To elucidate the structural basis for RNA binding, the solution structure of the Vts1 SAM domain, in the presence of a specific target RNA, has been solved by multidimensional heteronuclear NMR spectroscopy. The Vts1 SAM domain retains the "core" five-helix-bundle architecture of traditional SAM domains, but has additional short helices at N and C termini, comprising a small substructure that caps the core helices. The RNA-binding surface of Vts1, determined by chemical shift perturbation, maps near the ends of three of the core helices, in agreement with mutational data and the electrostatic properties of the molecule. These results provide a structural basis for the versatility of the SAM domain in protein and RNA-recognition.

Original languageEnglish (US)
Pages (from-to)1065-1072
Number of pages8
JournalJournal of Molecular Biology
Issue number5
StatePublished - Mar 10 2006
Externally publishedYes


  • RNA-binding protein
  • SAM domain
  • Smaug
  • Translational control
  • Vts1

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology


Dive into the research topics of 'Solution structure of the Vts1 SAM domain in the presence of RNA'. Together they form a unique fingerprint.

Cite this