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

Détails

ID Serval
serval:BIB_60116B67F371
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Purification, characterization and reassembly of the bacteriophage T4D tail sheath protein P18.
Périodique
Journal of Molecular Biology
Auteur(s)
Tschopp J., Arisaka F., van Driel R., Engel J.
ISSN
0022-2836 (Print)
ISSN-L
0022-2836
Statut éditorial
Publié
Date de publication
1979
Volume
128
Numéro
2
Pages
247-258
Langue
anglais
Résumé
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.
Mots-clé
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
Création de la notice
24/01/2008 16:18
Dernière modification de la notice
20/08/2019 15:17
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