A novel transposon, Tn6009, composed of a Tn916 element linked with a Staphylococcus aureus mer operon

O. O. Soge; N. K. Beck; T. M. White; D. B. No; M. C. Roberts

doi:10.1093/jac/dkn255

Deletion mutant analysis of the Staphylococcus aureus plasmid pI258 mercury-resistance determinant

Canadian Journal of Microbiology ◽

10.1139/m91-106 ◽

1991 ◽

Vol 37 (8) ◽

pp. 624-631 ◽

Cited By ~ 16

Author(s):

Kenneth Babich ◽

Mike Engle ◽

Jeffery S. Skinner ◽

Richard A. Laddaga

Keyword(s):

Staphylococcus Aureus ◽

Ion Transport ◽

Copy Number ◽

Deletion Mutant ◽

Resistance Determinant ◽

Mercury Resistance ◽

Mutant Analysis ◽

Mer Operon ◽

Copy Number Plasmid ◽

High Copy Number Plasmid

Deletion mutant analysis of the mercury-resistant determinant (mer operon) from the Staphylococcus aureus plasmid pI258 was used to verify the location of the merA and merB genes and to show the existence of mercuric ion transport gene(s). ORF5 was confirmed to be a transport gene and has an amino acid product sequence homologous to the merT gene products from several gram-negative bacteria and a Bacillus species. Deletion analysis established that inactivation of merA on a broad-spectrum mer resistance determinant resulted in a mercury-hypersensitive phenotype. Gene dosage had no apparent effect on the level of resistance conferred by the intact mer operon or on the expression of an inducible phenotype, except that when the intact pI258 mer operon was on a high copy number plasmid, uninduced cells possessed a volatilization rate that was at most only 3.5-fold less than that observed for induced cells. There was no need for mercury ion transport proteins for full resistance when the mer operon was expressed in a high copy number plasmid. Key words: mercury resistance, Staphylococcus aureus plasmid.

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Identification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon

Biochemistry ◽

10.1021/bi00135a020 ◽

1992 ◽

Vol 31 (20) ◽

pp. 4882-4891 ◽

Cited By ~ 17

Author(s):

Lynda B. M. Ellis ◽

Peter Saurugger ◽

Clare Woodward

Keyword(s):

Staphylococcus Aureus ◽

Three Dimensional ◽

Related Structure ◽

Mer Operon ◽

Orf3 Protein

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Cytochemical Studies of Cell Wall Biosynthesis in Staphylococcus Aureus

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100094905 ◽

1972 ◽

Vol 30 ◽

pp. 328-329

Author(s):

Masaatsu Koike ◽

Koichi Nakashima ◽

Kyoko Iida

Keyword(s):

Staphylococcus Aureus ◽

Periodate Oxidation ◽

Early Time ◽

The Other ◽

Penicillin G ◽

Cell Wall Biosynthesis ◽

Septal Wall ◽

Peptidoglycan Biosynthesis ◽

Gram Positive Bacteria ◽

Cross Linkage

Penicillin exerts the activity to inhibit the peptide cross linkage between each polysaccharide backbone at the final stage of wall-peptidoglycan biosynthesis of bacteria. Morphologically, alterations of the septal wall and mesosome in gram-positive bacteria, which were occurred in early time after treatment with penicillin, have been observed. In this experiment, these alterations were cytochemically investigated by means of silver-methenamine staining after periodate oxidation, which is applied for detection of localization of wall mucopolysaccharide.Staphylococcus aureus strain 209P treated with 100 u/ml of penicillin G was divided into two aliquotes. One was fixed by Kellenberger-Ryter's OSO4 fixative at 30, 60 and 120 min after addition of the antibiotic, dehydrated through alcohol series, and embedded in Epon 812 (Specimen A). The other was fixed by 21 glutaraldehyde, dehydrated through glycolmethacrylate series and embedded in glycolmethacrylate mixture, according to Bernhard's method (Specimen B).

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Gold labeling of teichoic acid on adjacent surfaces of staphylococcus aureus

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100160443 ◽

1990 ◽

Vol 48 (3) ◽

pp. 578-579

Author(s):

Margaret Hukee

Keyword(s):

Staphylococcus Aureus ◽

Teichoic Acid ◽

Protein Labeling ◽

Minimal Amount ◽

Section Thickness ◽

Double Labeling ◽

Parallel Surfaces ◽

Supporting Membrane

Gold labeling of two antigens (double labeling) is often done on two section surfaces separated by section thickness. Whether labeling is done on both sides of the same section or on two parallel surfaces separated by section thickness (PSSST), comparable results are dependent on an equal number of epitopes being exposed at each surface. We propose a method to study protein labeling within the same field of proteins, by examining two directly adjacent surfaces that were split during sectioning. The number of labeling sites on adjacent surfaces (AS) were compared to sites on PSSST surfaces in individual bacteria.Since each bacteria needed to be recognizable in all three section surfaces, one-hole grids were used for labeling. One-hole grids require a supporting membrane and excessive handling during labeling often ruptures the membrane. To minimize handling, a labeling chamber was designed that is inexpensive, disposable, minimizes contamination, and uses a minimal amount of solution.

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