Pseudomonas aeruginosa Pyoverdin: Structure and Function

2015 ◽  
pp. 8-14 ◽  
Author(s):  
Mohamed A. Abdallah ◽  
Martina Pfestorf ◽  
Gerd D�ring
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Structure And Function ◽  
And Function

scholarly journals PelX is a UDP-N-acetylglucosamine C4-epimerase involved in Pel polysaccharide–dependent biofilm formation

2020 ◽  
Vol 295 (34) ◽  
pp. 11949-11962 ◽  
Author(s):  
Lindsey S. Marmont ◽  
Gregory B. Whitfield ◽  
Roland Pfoh ◽  
Rohan J. Williams ◽  
Trevor E. Randall ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Biofilm Formation ◽  
Potential Role ◽  
Bacterial Species ◽  
Gene Clusters ◽  
Structure And Function ◽  
Bacterial Polysaccharide ◽  
H Nmr ◽  
Short Chain Dehydrogenase ◽  
And Function

Pel is a GalNAc-rich bacterial polysaccharide that contributes to the structure and function of Pseudomonas aeruginosa biofilms. The pelABCDEFG operon is highly conserved among diverse bacterial species, and Pel may therefore be a widespread biofilm determinant. Previous annotation of pel gene clusters has helped us identify an additional gene, pelX, that is present adjacent to pelABCDEFG in >100 different bacterial species. The pelX gene is predicted to encode a member of the short-chain dehydrogenase/reductase (SDR) superfamily, but its potential role in Pel-dependent biofilm formation is unknown. Herein, we have used Pseudomonas protegens Pf-5 as a model to elucidate PelX function as Pseudomonas aeruginosa lacks a pelX homologue in its pel gene cluster. We found that P. protegens forms Pel-dependent biofilms; however, despite expression of pelX under these conditions, biofilm formation was unaffected in a ΔpelX strain. This observation led us to identify a pelX paralogue, PFL_5533, which we designate here PgnE, that appears to be functionally redundant to pelX. In line with this, a ΔpelX ΔpgnE double mutant was substantially impaired in its ability to form Pel-dependent biofilms. To understand the molecular basis for this observation, we determined the structure of PelX to 2.1 Å resolution. The structure revealed that PelX resembles UDP-GlcNAc C4-epimerases. Using 1H NMR analysis, we show that PelX catalyzes the epimerization between UDP-GlcNAc and UDP-GalNAc. Our results indicate that Pel-dependent biofilm formation requires a UDP-GlcNAc C4-epimerase that generates the UDP-GalNAc precursors required by the Pel synthase machinery for polymer production.

scholarly journals Theoretical ribosomal protein mass distribution of Pseudomonas aeruginosa PAO1

2018 ◽  
Author(s):  
Wenfa Ng
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Small Subunit ◽  
Structure And Function ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
And Function ◽  
Unique Mass ◽  
Tof Ms

Ribosomes are the protein synthesis factories of a cell and thus are evolutionary conserved in structure and function. Comprising a large and small subunit, the ribosome is further made up of ribosomal proteins that give structure and function to different parts of the macromolecular complex. Current methods for isolating the ribosome include density gradient ultracentrifugation that separates the ribosome into the large and small subunit. Separation of the various ribosomal proteins that comprise each of the subunit would require a solubilization step followed by the use of sodium dodecyl sulphate and polyacrylamide gel electrophoresis (SDS-PAGE). However, possibility exists for the use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to profile the set of ribosomal proteins that could be solubilized from each ribosome subunit. Using ribosomal protein amino acid sequence information from Kyoto Encyclopaedia of Genes and Genomes (KEGG), the molecular weight of each ribosomal protein from Pseudomonas aeruginosa PAO1 was calculated in this report. Obtained results revealed that each ribosomal protein had a unique mass that could be detected by mid-range MALDI-TOF MS instruments. More importantly, the mass of ribosomal proteins constitutes a unique mass fingerprint of each ribosome subunit, which accounts for the different structure and functions of the large and small ribosome subunit. Overall, current mass resolution of MALDI-TOF MS instruments could resolve ribosomal proteins and thus provides a tool for profiling the set of ribosomal proteins that constitute the large and small subunit of the ribosome.

Uncovering the structure and function of Pseudomonas aeruginosa periplasmic proteins by an in silico approach

2019 ◽  
Vol 38 (15) ◽  
pp. 4508-4520
Author(s):  
Silvia Caprari ◽  
Valentina Brandi ◽  
Andrea Pasquadibisceglie ◽  
Fabio Polticelli
Keyword(s):  
Pseudomonas Aeruginosa ◽  
In Silico ◽  
Structure And Function ◽  
Periplasmic Proteins ◽  
And Function

scholarly journals Theoretical ribosomal protein mass distribution of Pseudomonas aeruginosa PAO1

2018 ◽  
Author(s):  
Wenfa Ng
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Small Subunit ◽  
Structure And Function ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
And Function ◽  
Unique Mass ◽  
Tof Ms

Ribosomes are the protein synthesis factories of a cell and thus are evolutionary conserved in structure and function. Comprising a large and small subunit, the ribosome is further made up of ribosomal proteins that give structure and function to different parts of the macromolecular complex. Current methods for isolating the ribosome include density gradient ultracentrifugation that separates the ribosome into the large and small subunit. Separation of the various ribosomal proteins that comprise each of the subunit would require a solubilization step followed by the use of sodium dodecyl sulphate and polyacrylamide gel electrophoresis (SDS-PAGE). However, possibility exists for the use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to profile the set of ribosomal proteins that could be solubilized from each ribosome subunit. Using ribosomal protein amino acid sequence information from Kyoto Encyclopaedia of Genes and Genomes (KEGG), the molecular weight of each ribosomal protein from Pseudomonas aeruginosa PAO1 was calculated in this report. Obtained results revealed that each ribosomal protein had a unique mass that could be detected by mid-range MALDI-TOF MS instruments. More importantly, the mass of ribosomal proteins constitutes a unique mass fingerprint of each ribosome subunit, which accounts for the different structure and functions of the large and small ribosome subunit. Overall, current mass resolution of MALDI-TOF MS instruments could resolve ribosomal proteins and thus provides a tool for profiling the set of ribosomal proteins that constitute the large and small subunit of the ribosome.

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