Purification, characterization and reassembly of the bacteriophage T4D tail sheath protein P18.

Details

Serval ID
serval:BIB_60116B67F371
Type
Article: article from journal or magazin.
Collection
Publications
Title
Purification, characterization and reassembly of the bacteriophage T4D tail sheath protein P18.
Journal
Journal of Molecular Biology
Author(s)
Tschopp J., Arisaka F., van Driel R., Engel J.
ISSN
0022-2836 (Print)
ISSN-L
0022-2836
Publication state
Published
Issued date
1979
Volume
128
Number
2
Pages
247-258
Language
english
Abstract
P18, the sole component of T4 tail sheath, has been isolated in a monomeric active form from extended sheaths of intact tails which were dissociated at low ionic strength. The molecular weight of P18 is determined to be 65,000 from sedimentation equilibrium and 73,000 from sodium dodecyl sulphate/gel electrophoresis. Combining the diffusion constant (D20,w = 5·5× 10−7cm2s−1)and the sedimentation constant (s020,w = 4·2 S) a value of 67,000 is obtained. The circular dichroism spectra reveal a striking similarity of the structure of P18 in the monomeric state and in the extended sheath conformation.
The purified P18 is found to reassemble into extended sheaths if the core-baseplate complex is present, forming normal length tails. Structures similar to polysheath are formed in the absence of core-baseplates.
Keywords
Amino Acids/analysis, Coliphages/analysis, Coliphages/ultrastructure, Electrophoresis, Polyacrylamide Gel, Microscopy, Electron, Molecular Weight, Morphogenesis, Protein Conformation, Viral Proteins/isolation & purification, Viral Proteins/metabolism
Pubmed
Web of science
Create date
24/01/2008 15:18
Last modification date
20/08/2019 14:17
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