Linked Life Data

11111919

Source:http://linkedlifedata.com/resource/pubmed/id/11111919

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4-5
pubmed:dateCreated
2001-4-19
pubmed:abstractText
The translocation of the pertussis toxin (PTX) S1 subunit into the cytoplasm of host cells was analysed in CHO cells producing S1 fused to a signal peptide. This protein channelled into the endoplasmic reticulum (ER) by the signal peptide, was found to ADP-ribosylate its target G proteins, suggesting that membrane translocation can occur from the ER and does not require the B oligomer. Similar results were obtained with a C-terminally truncated S1 subunit, indicating that this hydrophobic tail is not involved in the translocation mechanism. We also analysed the activity of two PTX mutants in which the S3 and S2 subunits were substituted for each other. The mutant protein containing two S3 subunits (PTXAS2) presented a decreased binding to fetuin or haptoglobin but higher in vivo activity than the wild-type PTX, suggesting that replacement of S2 by S3 favours the targeting of PTX to the compartment where translocation occurs and/or the dissociation of S1 from the B oligomer, thereby leading to a better translocation of S1 into the cytoplasm.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1438-4221
pubmed:author
pubmed:issnType
Print
pubmed:volume
290
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
409-13
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Intracellular trafficking and membrane translocation of pertussis toxin into host cells.
pubmed:affiliation
INSERM U447, Institut Pasteur de Lille, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't