Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions |
umls-concept:C0009282,
umls-concept:C0014834,
umls-concept:C0033684,
umls-concept:C0040715,
umls-concept:C0205147,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C0699788,
umls-concept:C1077660,
umls-concept:C1314939,
umls-concept:C1514562,
umls-concept:C1522702,
umls-concept:C1704675,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
pubmed:issue |
1
|
pubmed:dateCreated |
1998-3-31
|
pubmed:abstractText |
Group A colicins need proteins of the Escherichia coli envelope Tol complex (TolA, TolB, TolQ and TolR) to reach their cellular target. The N-terminal domain of colicins is involved in the import process. The N-terminal domains of colicins A and E1 have been shown to interact with TolA, and the N-terminal domain of colicin E3 has been shown to interact with TolB. We found that a pentapeptide conserved in the N-terminal domain of all group A colicins, the 'TolA box', was important for colicin A import but was not involved in the colicin A-TolA interaction. It was, however, involved in the colicin A-TolB interaction. The interactions of colicin A N-terminal domain deletion mutants with TolA and TolB were investigated. Random mutagenesis was performed on a construct allowing the colicin A N-terminal domain to be exported in the bacteria periplasm. This enabled us to select mutant protein domains unable to compete with the wild-type domain of the entire colicin A for import into the cells. Our results demonstrate that different regions of the colicin A N-terminal domain interact with TolA and TolB. The colicin A N-terminal domain was also shown to form a trimeric complex with TolA and TolB.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Colicins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Periplasmic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/tolA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/tolB protein, E coli
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0950-382X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
27
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
143-57
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9466263-Bacterial Proteins,
pubmed-meshheading:9466263-Blotting, Western,
pubmed-meshheading:9466263-Colicins,
pubmed-meshheading:9466263-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9466263-Escherichia coli,
pubmed-meshheading:9466263-Escherichia coli Proteins,
pubmed-meshheading:9466263-Membrane Proteins,
pubmed-meshheading:9466263-Mutagenesis,
pubmed-meshheading:9466263-Periplasmic Proteins,
pubmed-meshheading:9466263-Phenotype,
pubmed-meshheading:9466263-Plasmids,
pubmed-meshheading:9466263-Polymerase Chain Reaction
|
pubmed:year |
1998
|
pubmed:articleTitle |
Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli.
|
pubmed:affiliation |
Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, CNRS, Marseille, France.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|