| Structure and assembly of the capsid of bacteriophage P22. | |
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MedLine Citation:
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PMID: 13434 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Identification of the genes and proteins involved in phage P22 formation has permitted a detailed analysis of particle assembly, revealing some unexpected aspects. The polymerization of the major coat protein (gene 5 product) into an organized capsid is directed by a scaffolding protein (gene 8 product) which is absent from mature phage. The resulting capsid structure (prohead) is the precursor for DNA encapsidation. All of the scaffolding protein exits from the prohead in association with DNA packaging. These molecules then recycle, directing further rounds of prohead assembly. The structure of the prohead has been studied by electron microscopy of thin sections of phage infected cells, and by low angle X-ray scattering of concentrated particles. The results show that the prohead is a double shell structure, or a ball within a shell. The inner ball or shell is composed of the scaffolding protein while the outer shell is composed of coat protein. The conversion from prohead to mature capsid is associated with an expansion of the coat protein shell. It is possible that the scaffolding protein molecules exit through the capsid lattice. When DNA encapsidation within infected cells is blocked by mutation, scaffolding protein is trapped in proheads and cannot recycle. Under these conditions, the rate of synthesis of gp8 increases, so that normal proheads continue to form. These results suggest that free scaffolding protein negatively regulates its own further synthesis, providing a coupling between protein synthesis and protein assembly. |
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Authors:
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J King; D Botstein; S Casjens; W Earnshaw; S Harrison; E Lenk |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Philosophical transactions of the Royal Society of London. Series B, Biological sciences Volume: 276 ISSN: 0962-8436 ISO Abbreviation: Philos. Trans. R. Soc. Lond., B, Biol. Sci. Publication Date: 1976 Nov |
Date Detail:
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Created Date: 1977-03-21 Completed Date: 1977-03-21 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 7503623 Medline TA: Philos Trans R Soc Lond B Biol Sci Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 37-49 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Capsid*
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metabolism DNA, Viral / biosynthesis Genes Genetics, Microbial Mutation Salmonella Phages* / metabolism Salmonella typhimurium* / ultrastructure Viral Proteins* / biosynthesis, metabolism |
| Chemical | |
Reg. No./Substance:
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0/DNA, Viral; 0/Viral Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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