Conformation of the ribosomal protein S1 of Thermus thermophilus in solution under different ionic conditions
Timchenko, A.A.; Shiriaev, V.M.; Fedorova, I.Iu.; Kihara, K.; Kimura, K.; Willumeit, R.; Garamus, V.M.; Selivanova, O.M.
Biofizika 52(2): 216-222
2007
ISSN/ISBN: 0006-3029 PMID: 17477047 Document Number: 610523
The structure of protein S1 of Thermus thermophilus (M = 61 kDa) in solution at low and moderate ionic strengths (0 M and 100 mM NaCl, respectively) has been studied by small-angle X-ray and neutron scattering. It was found that protein S1 has a globular conformation under both ionic conditions. The modelling of different packing of six homologous domains of S1 on the basis of the NMR-resolved structure of one domain showed that the best fit of calculated scattering patterns from such complexes to experimental ones is observed at a compact package of the domains. The calculated value of the radius of gyration of the models is 28-29 angstrom, which is characteristic for globular proteins with a molecular mass of about 60 kDa. It was found that protein S1 has a tendency to form associates, and the type of the associate depends on ionic strength. These associates have, in general, two or three monomers at a moderate ionic strength, while at a low ionic strength the number of monomers exceeds three and they are packed in a compact manner. Strongly elongated associates were observed in neutron experiments at a moderate ionic strength in heavy water. The association of protein molecules was also confirmed by the data of dynamic light scattering. From these data, the translational diffusion coefficient of protein S1 at a moderate ionic strength was calculated to be (D-20,D-w= (2.7 +/- 0.1)center dot 10(-7)cm(2)/s). This value is essentially smaller than the expected value (D-20,D-w = (5.8 - 6.0)center dot 10(-7)cm(2)/s) for the S1 monomer in the globular conformation, indicating the association of protein molecules under equilibrium conditions.