Linked Life Data

9312085

Source:http://linkedlifedata.com/resource/pubmed/id/9312085

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
1997-10-22
pubmed:abstractText
The nature of the involvement of an intact NH2 terminus in the assembly of alpha-hemolysin of Staphylococcus aureus was reinvestigated. For the first time, a deletion of the first four amino acids at the NH2 terminus of alpha-hemolysin yielded a novel mutant that undergoes all of the conformational changes to form a lytic pore. The experimental evidence shows unequivocally that the mutant toxin forms heat- and sodium dodecyl sulfate-stable heptameric oligomers. The concentration required to achieve 50% lysis of red blood cells is around 58-116 ng/ml, and the time taken to achieve lysis to the same extent as that of intact toxin is considerably longer. Transmission electron microscopic studies also suggest that the pores formed by this deletion mutant are similar to those by the full-length toxin. This is in contrast to the previously reported 2- and 11-amino acid deletions that failed to proceed further from a presumed prefinal nonlytic pore to a lytic pore. Studies on the kinetics of assembly indicate that this mutant can form heat- and sodium dodecyl sulfate-stable oligomers as fast as full-length alpha-hemolysin but that pore opening is slowed down. The data strongly suggest that these amino acids (Ala-Asp-Ser-Asp) are involved in the final stages of assembly of alpha-hemolysin in target membranes.
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
3
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24858-63
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The role of the amino terminus in the kinetics and assembly of alpha-hemolysin of Staphylococcus aureus.
pubmed:affiliation
Institute of Microbial Technology, Sector 39A, Chandigarh 160 036, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't