EcoliWiki - User contributions [en]

PMID:1943697

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'''Russel, M ''' (1991) Filamentous phage assembly. ''Mol. Microbiol.'' '''5''':1607-13
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!align=left |Abstract
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Filamentous phages present a genetically well-defined system for studying the ordered membrane assembly of five different phage-encoded proteins around the circular single-stranded DNA phage genome. Assembly occurs at high efficiency in vivo, catalysed by two phage-encoded membrane proteins and at least one host protein, thioredoxin. This review presents a description of the virion and its cytoplasmic precursor and summarizes the results of genetic and biochemical experiments that are beginning to elucidate the role of the three morphogenetic proteins. The recent discovery of bacterial transport proteins with homology to a phage morphogenetic protein located in the outer membrane suggests the existence of a common mechanism for moving complex macromolecules across bacterial membranes.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1943697 PubMed]

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!align=left |Keywords
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Amino Acid Sequence; Bacteriophages/genetics; Bacteriophages/growth & development; DNA, Single-Stranded/biosynthesis; Escherichia coli/physiology; Genes, Viral; Macromolecular Substances; Molecular Sequence Data; Morphogenesis; Thioredoxins; Transduction, Genetic; Viral Proteins/biosynthesis; Viral Regulatory and Accessory Proteins

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==Significance {{HelpIcon|Help:Literature}} ==
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:1943697

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PMID:9636697

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'''Haigh, NG and Webster, RE ''' (1998) The major coat protein of filamentous bacteriophage f1 specifically pairs in the bacterial cytoplasmic membrane. ''J. Mol. Biol.'' '''279''':19-29
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Filamentous bacteriophage are long, thin single-stranded DNA viruses that infect male strains of Escherichia coli without killing the host. Each phage contains approximately 2700 copies of the major coat protein, pVIII, which exists as a 5.2 kDa cytoplasmic membrane protein prior to incorporation into phage. Studies from a number of groups analyzing the behavior of wild-type and mutant pVIII in detergents suggested that pVIII might pair under these conditions. In order to test whether pVIII molecules pair in vivo in the cytoplasmic membrane, four plasmidencoded pVIII variants were constructed in which specific residues in the transmembrane region were mutated to cysteine in an attempt to stabilize any pair via disulfide bridges. Variants A35C and I39C were unable to complement phage with an amber mutation in gene VIII. The I39C variant was unable to be packaged into phage particles even though it was inserted into the membrane. In the case of A35C, the inability to complement was not due to a packaging defect because the variant protein could be packaged into phage in the presence of wild-type pVIII. Western blot analysis of cytoplasmic membrane samples revealed that the A35C variant formed stable disulfide dimers in vivo. Expression of A35C interfered with wild-type phage infection, indicating that the assembly machinery may recognize the disulfide dimers in some non-productive way. The results indicate that pVIII may specifically pair along a particular face in the cytoplasmic membrane prior to assembly; however, these pairs must be able to be separated in order for normal assembly to occur.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9636697 PubMed]
Online version:[http://dx.doi.org/10.1006/jmbi.1998.1778 10.1006/jmbi.1998.1778]
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!align=left |Keywords
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Bacteriophages/chemistry; Bacteriophages/growth & development; Bacteriophages/metabolism; Blotting, Western; Capsid/metabolism; Cell Membrane/metabolism; Escherichia coli/metabolism; Escherichia coli/virology; Mutation; Viral Plaque Assay; Viral Proteins/chemistry; Viral Proteins/immunology; Viral Proteins/metabolism

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==Significance {{HelpIcon|Help:Literature}} ==
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:9636697

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PMID:4979697

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'''Marvin, DA and Hohn, B ''' (1969) Filamentous bacterial viruses. ''Bacteriol Rev'' '''33''':172-209
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No abstract in PubMed
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4979697 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC378320 PMC378320]

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Bacteriolysis; Bacteriophages/classification; Biometry; Coliphages; DNA Replication; DNA Viruses; DNA, Viral; Escherichia coli; Genes; Genetics, Microbial; Microscopy, Electron; Mutation; Pseudomonas aeruginosa; Salmonella Phages; Salmonella typhimurium; Templates, Genetic; Vibrio; Viral Proteins; Virus Replication; X-Ray Diffraction; Xanthomonas

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==Significance {{HelpIcon|Help:Literature}} ==
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{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="J5130133152f7a" class=" tableEdit GO_table_reference dataTable"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:4979697

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PMID:9224870

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'''Russel, M , Linderoth, NA and Sali, A ''' (1997) Filamentous phage assembly: variation on a protein export theme. ''Gene'' '''192''':23-32
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Biogenesis of both filamentous phage and type-IV pili involves the assembly of many copies of a small, integral inner membrane protein (the phage major coat protein or pilin) into a helical, tubular array that passes through the outer membrane. The occurrence of related proteins required for assembly and export in both systems suggests that there may be similarities at the mechanistic level as well. This report summarizes the properties of filamentous phage and the proteins required for their assembly, with particular emphasis on features they may share with bacterial protein export and pilus biogenesis systems, and it presents evidence that supports the hypothesis that one of the phage proteins functions as an outer membrane export channel.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9224870 PubMed]

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Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacteriophages/genetics; Bacteriophages/metabolism; Biological Transport/physiology; Fimbriae Proteins; Fimbriae, Bacterial/genetics; Fimbriae, Bacterial/metabolism; Genes, Viral; Protein Conformation; Sequence Alignment; Viral Proteins/metabolism

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==Significance {{HelpIcon|Help:Literature}} ==
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<protect>

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="C513012b909dc1" class=" tableEdit GO_table_reference dataTable"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:9224870

2013-03-01T02:30:16Z

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PMID:9631287

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'''Marvin, DA ''' (1998) Filamentous phage structure, infection and assembly. ''Curr. Opin. Struct. Biol.'' '''8''':150-8
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The structural model of filamentous phage derived by X-ray fibre diffraction is supported by spectroscopic and genetic experiments. The structure of the receptor-binding domain at the end of the phage and the structure of the phage-coded intracellular DNA-binding protein have been determined at high resolution. The recent dissection of the virus life cycle by genetic and biochemical analyses, combined with structural information, suggests models for virus infection and assembly.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9631287 PubMed]

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!align=left |Keywords
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Amino Acid Sequence; Bacteriophages/chemistry; Bacteriophages/growth & development; Bacteriophages/pathogenicity; Capsid/chemistry; Capsid/genetics; DNA, Viral/chemistry; Gram-Negative Bacteria/virology; Models, Biological; Models, Molecular; Molecular Sequence Data; X-Ray Diffraction

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

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<protect>

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="A5130127d29e77" class=" tableEdit GO_table_reference dataTable"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:9631287

2013-03-01T02:29:16Z

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PMID:21082179

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'''Straus, SK , Scott, WR , Schwieters, CD and Marvin, DA ''' (2011) Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR. ''Eur. Biophys. J.'' '''40''':221-34
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!align=left |Abstract
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Filamentous bacteriophages (filamentous bacterial viruses or Inovirus) are simple and well-characterised macromolecular assemblies that are widely used in molecular biology and biophysics, both as paradigms for studying basic biological questions and as practical tools in areas as diverse as immunology and solid-state physics. The strains fd, M13 and f1 are virtually identical filamentous phages that infect bacteria expressing F-pili, and are sometimes grouped as the Ff phages. For historical reasons fd has often been used for structural studies, but M13 and f1 are more often used for biological experiments. Many other strains have been identified that are genetically quite distinct from Ff and yet have a similar molecular structure and life cycle. One of these, Pf1, gives the highest resolution X-ray fibre diffraction patterns known for filamentous bacteriophage. These diffraction patterns have been used in the past to derive a molecular model for the structure of the phage. Solid-state NMR experiments have been used in separate studies to derive a significantly different model of Pf1. Here we combine previously published X-ray fibre diffraction data and solid-state NMR data to give a consensus structure model for Pf1 filamentous bacteriophage, and we discuss the implications of this model for assembly of the phage at the bacterial membrane.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21082179 PubMed]
Online version:[http://dx.doi.org/10.1007/s00249-010-0640-9 10.1007/s00249-010-0640-9]
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Bacteriophage Pf1/chemistry; Bacteriophage Pf1/metabolism; Capsid/chemistry; Capsid Proteins/chemistry; Cell Membrane/chemistry; Magnetic Resonance Spectroscopy/methods; Models, Molecular; Protein Conformation; Pseudomonas/virology; Viral Proteins/chemistry; Virion/chemistry; X-Ray Diffraction/methods

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==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

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{{LitMaterials}}

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<protect>

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="E513012411324f" class=" tableEdit GO_table_reference dataTable"
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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PMID:21082179

2013-03-01T02:28:16Z

85.25.176.105: New PMID: Page!