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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
1989-4-25
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pubmed:abstractText |
The expression of cloned bacteriophage phi X174 lysis gene E was analyzed in minicells of Escherichia coli using two-dimensional gel electrophoresis. Beside the 10-11-kDa protein-E, at least two additional protein bands were detected, associated with the inner membrane, which showed the same isoelectric point as E. To clarify whether these proteins were E-specific, two different antibodies directed against a beta-galactosidase-E' hybrid protein and a synthetic oligopeptide corresponding to the C-terminal end of protein-E were raised. Immunoadsorption studies with anti-peptide-specific antibodies resulted in the detection of protein-E as well as in the detection of proteins of higher molecular weight. Two of these protein bands were positively recognized by anti beta-galactosidase-E' antibodies. The latter protein bands had the same molecular weight as the putative protein-E bands detected by two-dimensional gel electrophoresis indicating that these bands represent protein-E-specific oligomers. These data support the idea that an E-specific oligomeric structure penetrating the inner and outer membrane of E. coli is formed during the lytic action of protein-E.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/E protein, bacteriophage X174,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
264
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4552-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2466836-Antibodies,
pubmed-meshheading:2466836-Antigens,
pubmed-meshheading:2466836-Bacterial Proteins,
pubmed-meshheading:2466836-Bacteriophage phi X 174,
pubmed-meshheading:2466836-Cell Membrane,
pubmed-meshheading:2466836-DNA, Viral,
pubmed-meshheading:2466836-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:2466836-Epitopes,
pubmed-meshheading:2466836-Escherichia coli,
pubmed-meshheading:2466836-Gene Expression Regulation,
pubmed-meshheading:2466836-Immunosorbent Techniques,
pubmed-meshheading:2466836-Macromolecular Substances,
pubmed-meshheading:2466836-Molecular Weight,
pubmed-meshheading:2466836-Oligopeptides,
pubmed-meshheading:2466836-Plasmids,
pubmed-meshheading:2466836-Promoter Regions, Genetic,
pubmed-meshheading:2466836-Recombinant Fusion Proteins,
pubmed-meshheading:2466836-Transformation, Bacterial,
pubmed-meshheading:2466836-Viral Proteins,
pubmed-meshheading:2466836-beta-Galactosidase
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pubmed:year |
1989
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pubmed:articleTitle |
Evidence for membrane-bound oligomerization of bacteriophage phi X174 lysis protein-E.
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pubmed:affiliation |
Institute of Genetics and Microbiology, University of Munich, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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