Effects of amino acid substitution on the thermal stability of MS2 capsids lacking genomic RNA

The thermal stability of capsids of the bacteriophage MS2, lacking genomic RNA, has been investigated using electron microscopy. Coat protein mutants with amino acid substitutions at residues involved in making contacts at both inter-molecular interfaces and within the coat protein subunit are also...

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Bibliographic Details
Published in:FEBS letters 1993-11, Vol.334 (3), p.355-359
Main Authors: Stonehouse, N.J., Stockley, P.G.
Format: Article
Language:English
Subjects:
Amino Acids - metabolism
Biological and medical sciences
Capsid - chemistry
Capsid - genetics
Capsid - metabolism
Capsid assembly
Electron microscopy
Fundamental and applied biological sciences. Psychology
Levivirus - genetics
Levivirus - metabolism
Levivirus - ultrastructure
Microscopy, Electron
Miscellaneous
Molecular biophysics
MS2
Mutagenesis
phage MS2
Physical chemistry in biology
Protein Conformation
RNA, Viral
Temperature
Thermal stability
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Summary:The thermal stability of capsids of the bacteriophage MS2, lacking genomic RNA, has been investigated using electron microscopy. Coat protein mutants with amino acid substitutions at residues involved in making contacts at both inter-molecular interfaces and within the coat protein subunit are also capable of forming ‘empty’ capsids of the same size and symmetry as the wild-type protein. Mutations have been characterised which are neutral, deleterious or advantageous in terms of thermal stability. In some cases, the results can be rationalised by reference to the recently refined X-ray crystal structure of the wild-type particle.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(93)80711-3