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Published online before print September 8, 2006, 10.1110/ps.062191506
Protein Science (2006), 15:2310-2317. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Oligomerization behavior of the archaeal Sm2-type protein from Archaeoglobus fulgidus

Turgay Kilic1, Sarah Sanglier2, Alain Van Dorsselaer2 and Dietrich Suck1

1 Structural and Computational Biology Programme, European Molecular Biology Laboratory (EMBL), 69117 Heidelberg, Germany
2 Laboratoire de Spectrométrie de Masse Bio-Organique, LC4-UMR7178 CNRS-Université Louis Pasteur, ECPM, F-67087 Strasbourg, France

(RECEIVED March 1, 2006; FINAL REVISION June 20, 2006; ACCEPTED July 7, 2006)

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.

Keywords: archaea; Sm-like protein; Sm fold; RNA binding; heptamer; hexamer; noncovalent mass spectrometry


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