Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1990-11-15
pubmed:abstractText
Upon binding of bacteriophage T5 tails to purified FhuA receptor protein the tail-tip protein pb2 became extremely sensitive to trypsin and other proteases. However, when T5 tails were bound to FhuA integrated into liposomes, pb2 was found to retain some resistance to trypsin. Electron microscopic examination of tail-liposome complexes supported the idea that trypsin resistance of pb2 in such complexes was caused by insertion of the tail-tip into the liposomes. pb2 was isolated from tails by treatment with sodium dodecyl sulfate and was further purified by gel filtration using a fast protein liquid chromatography system. pb2 obtained with this procedure was most likely monomeric. It was extremely sensitive to trypsin. When reconstituted into black lipid bilayer membranes, it formed pores with an average single-channel conductance of 4.6 nanosiemens in 1 M KCl. Zero-current potential measurements showed only a very slight preference, if any, for cations over anions. The data are compatible with pb2 forming a large water-filled transmembrane channel. The functioning during infection of pb2 in cytoplasmic membrane depolarization and phage DNA uptake into the cell is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:geneSymbol
fhuA
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18561-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Pore formation associated with the tail-tip protein pb2 of bacteriophage T5.
pubmed:affiliation
Fakultät für Biologie, Universität Konstanz, Federal Republic of Germany.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't