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Article Dans Une Revue Virology Année : 1996

Bacteriophage Mu head assembly

Résumé

The protein composition of defective particles produced by various bacteriophage Mu head-gene mutants was analyzed by SDS-PAGE. An abundant 20-kDa protein was detected in only one type of defective head. This protein exhibits properties of a scaffolding protein. A 50-kDa structural protein present in most defective heads was shown to be produced by cleavage of the C-terminus of the 64-kDa polypeptide encoded by gene H. Cleavage occurs during head assembly at a site which, according to earlier results, might separate two different functional domains in gpH. A fraction of the gpH molecules produced upon Mu induction sediment in a 25 S complex, suggesting that gpH participates in the formation of an early intermediate of Mu head assembly. Characteristics of gpH suggest that it may be the Mu portal protein.

Domaines

Virologie

Dates et versions

hal-01614795 , version 1 (14-03-2024)

Identifiants

Citer

Régis Grimaud. Bacteriophage Mu head assembly. Virology, 1996, 217 (1), pp.200-210. ⟨10.1006/viro.1996.0107⟩. ⟨hal-01614795⟩
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