Linked Life Data

7934926

Source:http://linkedlifedata.com/resource/pubmed/id/7934926

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1994-11-14
pubmed:abstractText
The 1706-residue adenylate cyclase toxin (CyaA) of Bordetella pertussis is an RTX protein with extensive carboxy-proximal glycine and aspartate-rich repeats. CyaA does not have a cleavable amino-terminal signal peptide and can be secreted across both bacterial membranes of the Escherichia coli cell envelope by the alpha-haemolysin (HlyA) translocator (HlyBD/TolC). We performed deletion mapping of secretion signals recognized in CyaA by this heterologous translocator. Truncated proteins with N-terminal and internal deletions were secreted at levels up to 10 times higher than intact CyaA and similar to HlyA. A secretion signal recognized by HlyBD/TolC was found within the last 74 residues of CyaA. However, secretion of CyaA was reduced but not abolished upon deletion of the last 75 or 217 residues, indicating that at least two additional secretion signals recognized by HlyBD/TolC are within CyaA. One of them was localized to the repeat sequence between residues Asp-1587 to Ile-1631. Interestingly, a conserved 'acidic' motif (Glu/Asp)-(X)11-Asp-(X)3/5-(Glu/Asp)-(X)14-Asp was found in the C-terminal sequences of HlyA, CyaA and the two secreted CyaA derivatives. We speculate that the presence and spacing of acidic residues may be an important feature of secretion signals recognized by the haemolysin translocator.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:geneSymbol
cyaA
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
999-1009
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7934926-Adenylate Cyclase, pubmed-meshheading:7934926-Adenylate Cyclase Toxin, pubmed-meshheading:7934926-Amino Acid Sequence, pubmed-meshheading:7934926-Bacterial Proteins, pubmed-meshheading:7934926-Bordetella pertussis, pubmed-meshheading:7934926-Conserved Sequence, pubmed-meshheading:7934926-Escherichia coli, pubmed-meshheading:7934926-Escherichia coli Proteins, pubmed-meshheading:7934926-Hemolysin Proteins, pubmed-meshheading:7934926-Molecular Sequence Data, pubmed-meshheading:7934926-Oligodeoxyribonucleotides, pubmed-meshheading:7934926-Plasmids, pubmed-meshheading:7934926-Protein Precursors, pubmed-meshheading:7934926-Repetitive Sequences, Nucleic Acid, pubmed-meshheading:7934926-Sequence Deletion, pubmed-meshheading:7934926-Sequence Homology, Amino Acid, pubmed-meshheading:7934926-Signal Transduction
pubmed:year
1993
pubmed:articleTitle
Repeat sequences in the Bordetella pertussis adenylate cyclase toxin can be recognized as alternative carboxy-proximal secretion signals by the Escherichia coli alpha-haemolysin translocator.
pubmed:affiliation
Unité de Biochimie des Régulations Cellulaires, Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't