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PMID:8599204
| Citation |
Grimaud, R (1996) Bacteriophage Mu head assembly. Virology 217:200-10 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1006/viro.1996.0107 |
| Keywords |
Bacteriophage mu/physiology; Centrifugation, Density Gradient; Defective Viruses/physiology; Electrophoresis, Polyacrylamide Gel; Genes, Viral; Viral Proteins/biosynthesis; Viral Proteins/genetics; Viral Proteins/isolation & purification; Virus Assembly |
Significance
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| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
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