Oligomerization behavior of the archaeal Sm2-type protein from Archaeoglobus fulgidus.
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.
Kilic
Turgay
T
Structural and Computational Biology Programme, European Molecular Biology Laboratory (EMBL), 69117 Heidelberg, Germany.
Sanglier
Sarah
S
Van Dorsselaer
Alain
A
Suck
Dietrich
D
D019843:Archaeal Proteins / Q000737:chemistry*; D019611:Archaeoglobus fulgidus / Q000737:chemistry*; D002850:Chromatography, Gel; D019281:Dimerization; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry; D012313:RNA / Q000494:pharmacology; D017411:Ribonucleoproteins, Small Nuclear / Q000737:chemistry*
D019843:Archaeal Proteins; D017411:Ribonucleoproteins, Small Nuclear; C426829:Sm2 protein, Archaeoglobus fulgidus; D012313:RNA