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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

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