Complementing structural information of modular proteins with small angle neutron scattering and contrast variation

Grossmann, J.G., Callaghan, A.J., Marcaida, M.J., Luisi, B.F., Alcock, F.H. and Tokatlidis, K. (2008) Complementing structural information of modular proteins with small angle neutron scattering and contrast variation. European Biophysics Journal with Biophysics Letters, 37(5), pp. 603-611. (doi:10.1007/s00249-008-0278-z)

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Abstract

Many macromolecules in the cell function by forming multi-component assemblies. We have applied the technique of small angle neutron scattering to study a nucleic acid–protein complex and a multi-protein complex. The results illustrate the versatility and applicability of the method to study macromolecular assemblies. The neutron scattering experiments, complementing X-ray solution scattering data, reveal that the conserved catalytic domain of RNase E, an essential ribonuclease in Escherichia coli (E. coli), undergoes a marked conformational change upon binding a 5′monophosphate–RNA substrate analogue. This provides the first evidence in support of an allosteric mechanism that brings about RNA substrate cleavage. Neutron contrast variation of the multi-protein TIM10 complex, a mitochondrial chaperone assembly comprising the subunits Tim9 and Tim10, has been used to determine a low-resolution shape reconstruction of the complex, highlighting the integral subunit organization. It shows characteristic features involving protrusions that could be assigned to the six subunits forming the complex.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Tokatlidis, Professor Kostas
Authors: Grossmann, J.G., Callaghan, A.J., Marcaida, M.J., Luisi, B.F., Alcock, F.H., and Tokatlidis, K.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:European Biophysics Journal with Biophysics Letters
Publisher:Springer-Verlag
ISSN:0175-7571
ISSN (Online):1432-1017

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