Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1994-1-13
pubmed:abstractText
The peptidoglycan of a Tn551 mutant of Staphylococcus aureus (RUSA208) selected for reduced methicillin resistance was analyzed by reversed-phase high pressure liquid chromatography and mass spectrometry. RUSA208 is a member of a cluster of Tn551 mutants located on fragment A of SmaI digests but is distinct from the femA and femB class of mutants. The peptidoglycan of RUSA208 contained normal parental muropeptides but in diminished amounts only. The major muropeptides of RUSA208 were new components eluting with somewhat longer retention times from the column. Amino acid analysis of these new muropeptides showed identical compositions to the corresponding peaks in the parental strain, but mass spectrometry revealed increased molecular weights by the following mass units: 1 (in monomers), 1 or 2 (in dimers), and 2 or 3 (in trimers). These observations suggest that in RUSA208 the mutational block may be in the amidation of the stem peptide glutamate residues, resulting in the replacement of isoglutamine with free glutamic acid in one or more of the cell wall stem peptides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26268-72
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The peptidoglycan composition of a Staphylococcus aureus mutant selected for reduced methicillin resistance.
pubmed:affiliation
Rockefeller University, New York, New York 10021.
pubmed:publicationType
Journal Article