scholarly journals Identification and Characterization of a Monofunctional Glycosyltransferase from Staphylococcus aureus

2001 ◽  
Vol 183 (16) ◽  
pp. 4779-4785 ◽  
Author(s):  
Q. May Wang ◽  
Robert B. Peery ◽  
Robert B. Johnson ◽  
William E. Alborn ◽  
Wu-Kuang Yeh ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Structural Elements ◽  
Homogeneity Analysis ◽  
Hydrophobic Domain ◽  
Penicillin Binding Proteins ◽  
Class A ◽  
Calculated Molecular Weight ◽  
Identification And Characterization ◽  
Secondary Structural Elements

ABSTRACT A gene (mgt) encoding a monofunctional glycosyltransferase (MGT) from Staphylococcus aureus has been identified. This first reported gram-positive MGT shared significant homology with several MGTs from gram-negative bacteria and the N-terminal glycosyltransferase domain of class A high-molecular-mass penicillin-binding proteins from different species.S. aureus MGT contained an N-terminal hydrophobic domain perhaps involved with membrane association. It was expressed inEscherichia coli cells as a truncated protein lacking the hydrophobic domain and purified to homogeneity. Analysis by circular dichroism revealed that secondary structural elements of purified truncated S. aureus MGT were consistent with predicted structural elements, indicating that the protein might exhibit the expected folding. In addition, purified S. aureus MGT catalyzed incorporation of UDP-N-acetylglucosamine into peptidoglycan, proving that it was enzymatically active. MGT activity was inhibited by moenomycin A, and the reaction product was sensitive to lysozyme treatment. Moreover, a protein matching the calculated molecular weight ofS. aureus MGT was identified from an S. aureus cell lysate using antibodies developed against purified MGT. Taken together, our results suggest that this enzyme is natively present in S. aureus cells and that it may play a role in bacterial cell wall biosynthesis.

In silico identification and characterization of sensory motifs in the transcriptional regulators of the ArsR-SmtB family

Metallomics ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 1476-1500 ◽  
Author(s):  
Rima Roy ◽  
Saikat Samanta ◽  
Surajit Patra ◽  
Nav Kumar Mahato ◽  
Rudra P. Saha
Keyword(s):  
In Silico ◽  
Transcriptional Regulators ◽  
Transcriptional Repressors ◽  
Structural Elements ◽  
In Silico Identification ◽  
Metal Efflux ◽  
Identification And Characterization ◽  
Secondary Structural Elements ◽  
Efflux Proteins

The ArsR-SmtB family of transcriptional repressors regulates the transcription of metal-efflux proteins by binding specific metals at a variety of secondary structural elements, called motifs, on the surface of the proteins.

scholarly journals Proteomic Characterization of Bacteriophage Peptides from the Mastitis Producer Staphylococcus aureus by LC-ESI-MS/MS and the Bacteriophage Phylogenomic Analysis

Foods ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 799
Author(s):  
Ana G. Abril ◽  
Mónica Carrera ◽  
Karola Böhme ◽  
Jorge Barros-Velázquez ◽  
Benito Cañas ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Dairy Products ◽  
Phylogenomic Analysis ◽  
Esi Ms ◽  
Complement Inhibitors ◽  
Staphylococcus Spp ◽  
The Relationship ◽  
Phage Proteins ◽  
Identification And Characterization

The present work describes LC-ESI-MS/MS MS (liquid chromatography-electrospray ionization-tandem mass spectrometry) analyses of tryptic digestion peptides from phages that infect mastitis-causing Staphylococcus aureus isolated from dairy products. A total of 1933 nonredundant peptides belonging to 1282 proteins were identified and analyzed. Among them, 79 staphylococcal peptides from phages were confirmed. These peptides belong to proteins such as phage repressors, structural phage proteins, uncharacterized phage proteins and complement inhibitors. Moreover, eighteen of the phage origin peptides found were specific to S. aureus strains. These diagnostic peptides could be useful for the identification and characterization of S. aureus strains that cause mastitis. Furthermore, a study of bacteriophage phylogeny and the relationship among the identified phage peptides and the bacteria they infect was also performed. The results show the specific peptides that are present in closely related phages and the existing links between bacteriophage phylogeny and the respective Staphylococcus spp. infected.

Identification and characterization of two novel superantigens among Staphylococcus aureus complex

2018 ◽  
Vol 308 (4) ◽  
pp. 438-446 ◽  
Author(s):  
Dao-Feng Zhang ◽  
Xin-Yi Yang ◽  
Jing Zhang ◽  
Xiaojie Qin ◽  
Xiaozhen Huang ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Identification And Characterization

scholarly journals Plasmid-mediated trimethoprim-resistance in Staphylococcus aureus. Characterization of the first gram-positive plasmid dihydrofolate reductase (type S1)

1987 ◽  
Vol 243 (1) ◽  
pp. 309-312 ◽  
Author(s):  
H K Young ◽  
R A Skurray ◽  
S G B Amyes
Keyword(s):  
Staphylococcus Aureus ◽  
Dihydrofolate Reductase ◽  
Specific Activity ◽  
Gram Positive ◽  
Heat Stable ◽  
Dihydrofolate Reductases ◽  
High Degree ◽  
Moderately Resistant ◽  
Identification And Characterization

The trimethoprim-resistance gene located on plasmid pSK1, originally identified in a multi-resistant Staphylococcus aureus from Australia, encodes the production of a dihydrofolate reductase (type S1), which confers a high degree of resistance to its host and is quite unlike any plasmid-encoded dihydrofolate reductase hitherto described. It has a low Mr (19,700) and has a higher specific activity than the constitutive Gram-negative plasmid dihydrofolate reductases. The type S1 enzyme is heat-stable and has a relatively low affinity for the substrate, dihydrofolate (Km 10.8 microM). It is moderately resistant to trimethoprim, and is competitively inhibited by this drug with an inhibitor-binding constant of 11.6 microM. This is the first identification and characterization of a plasmid-encoded trimethoprim-resistant dihydrofolate reductase derived from a Gram-positive species.

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