Oligomerization behavior of the archaeal Sm2-type protein from Archaeoglobus fulgidus.
Fiche publication
Date publication
octobre 2006
Auteurs
Membres identifiés du Cancéropôle Est :
Dr CIANFERANI Sarah, Dr VAN DORSSELAER Alain
Tous les auteurs :
Kilic T, Sanglier S, Van Dorsselaer A, Suck D
Lien Pubmed
Résumé
As part of a functional analysis of archaeal Sm-related proteins, we have studied the oligomerization behavior of the Sm-2 type protein from the euryarchaeon Archaeoglobus fulgidus using gel filtration chromatography and noncovalent mass spectrometry. Our experiments show that the oligomeric state of the protein depends on the pH and presence of RNA. The protein forms a hexamer at acidic pH in the absence of RNA. The addition of RNA (oligo U10) induces the formation of a heptamer over the whole pH range studied. The stability of both the hexamer and the RNA-bound heptamer increases at lower pH.
Référence
Protein Sci. 2006 Oct;15(10):2310-7