Reassembly of the bacteriophage T4 tail from the core-baseplate and the monomeric sheath protein P18: a co-operative association process.

Details

Serval ID
serval:BIB_BAA7CFF3EFAE
Type
Article: article from journal or magazin.
Collection
Publications
Title
Reassembly of the bacteriophage T4 tail from the core-baseplate and the monomeric sheath protein P18: a co-operative association process.
Journal
Journal of Molecular Biology
Author(s)
Arisaka F., Tschopp J., Van Driel R., Engel J.
ISSN
0022-2836 (Print)
ISSN-L
0022-2836
Publication state
Published
Issued date
1979
Volume
132
Number
3
Pages
369-386
Language
english
Abstract
The reassociation of the monomeric sheath protein, the product of gene 18, with the core-baseplate was investigated by analytical ultracentrifugation, light-scattering and electron microscopy.
The following conclusions are reached: (1) monomeric P18 molecules are in equilibrium with the extended tail sheath; (2) the association process is co-operative and the critical concentration of P18 is about 0.4 μm in the presence of 0.1 m-KCl in 1 mm-potassium phosphate buffer (pH 7.0 at 20 °C); (3) binding of P18 to the baseplate-core junction is the initial stop in extended sheath formation; (4) slow, irreversible polysheath formation competes with the assembly of extended sheath, but the latter is kinetically much more favored.
Model calculations on the isotherm of the sheath formation and on the length distribution strongly suggest a rate-limiting nucleation step, and a distinctly strong binding of the last annulus of the sheath to the core-baseplate.
Keywords
Kinetics, Light, Microscopy, Electron, Models, Biological, Morphogenesis, Scattering, Radiation, T-Phages/growth & development, T-Phages/ultrastructure, Thermodynamics, Ultracentrifugation, Viral Proteins
Pubmed
Web of science
Create date
24/01/2008 15:19
Last modification date
20/08/2019 15:28
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