Li, FEBS Letters, 2007

FEBS Lett. 2007 Dec 11;581(29):5698-702. Epub 2007 Nov 26.

Related Articles, Links

Mutations of the SM protein Sly1 resulting in bypass of GTPase requirement in vesicular transport are confined to a short helical region.

Li Y, Schmitt HD, Gallwitz D, Peng RW.

Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, 37070 Göttingen, Germany.

SLY1-20 is a suppressor of Ypt1p lethality. It is essential for membrane fusion and appears to coordinate the function of Ypt1 and SNAREs. Mutations in the alpha helix 20 (T531 or E532) or complete deletion of E532 or the whole helix result in bypass of Ypt1 or Ypt6. Hypothesis that this helix is normally closed, protecting a conserved helical region (helices 13 and 14) of sly1p domain, these mutations are postulated to keep the "lid" constitutively open. Helix 20 and the TE/TD motif are conserved in fungi, but not in multi-cellular organisms