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אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
Fate of predator and prey proteins during growth of Bdellovibrio bacteriovorus on Escherichia coli and Pseudomonas syringae prey
Year:
2005
Source of publication :
Journal of Bacteriology
Authors :
בראל, גילי
;
.
Volume :
187
Co-Authors:
Barel, G., Dept. of Plant Pathol./Microbiol., Fac. Agric., Food/Environ. Qual. S., Hebrew University of Jerusalem, Rehovot, Israel
Sirota, A., Dept. of Genomics and Bioinformatics, Agricultural Research Organization, Bet Dagan, Israel
Volpin, H., Dept. of Genomics and Bioinformatics, Agricultural Research Organization, Bet Dagan, Israel
Jurkevitch, E., Dept. of Plant Pathol./Microbiol., Fac. Agric., Food/Environ. Qual. S., Hebrew University of Jerusalem, Rehovot, Israel, Dept. of Plant Pathol./Microbiol., Fac. Agric., Food/Environ. Qual. S., Hebrew University of Jerusalem, P.O. Box 12, 76100 Rehovot, Israel
Facilitators :
From page:
329
To page:
335
(
Total pages:
7
)
Abstract:
A two-dimensional electrophoretic analysis of protein distribution followed by identification of selected proteins by mass spectrometry was performed on fresh bdellovibrio cultures containing attack phase cells of the predatory bacterium Bdellovibrio bacteriovorus strain 109J-1 and the remains of an Escherichia coli or a Pseudomonas syringae pv. tomato prey. Cleavage of the peptidoglycan-associated outer membrane proteins (OMPs) OmpA in E. coli and OprF in P. syringae occurred in both prey. The tryptic peptides obtained from the cleavage products of OmpA and OprF were all located within the 19-kDa pronase-resistant N-terminal parts of the corresponding proteins. The predator cell fraction was separated from the prey ghosts in fresh bdellovibrio cultures by centrifugation on a Percoll-sucrose cushion. Proteins from each fraction were separated by two-dimensional electrophoresis and identified by mass spectrometric analysis. As no prey OMP could be detected in the predator cell fraction, it was concluded that prey OMPs are not transferred to the predator, as had been suggested previously. However, a protein from the predator was found bound to ghost cell envelopes. This protein may correspond to a protein earlier suggested to be associated with the prey outer or cytoplasmic membranes. Along with recently described polypeptides from B. bacteriovorus strains 100 and 114, it forms a new family of putative outer membrane proteins.
Note:
Related Files :
Bacterial Outer Membrane Proteins
cell membrane
Electrophoresis
outer membrane protein regulator
Pseudomonas syringae pv. tomato
עוד תגיות
תוכן קשור
More details
DOI :
10.1128/JB.187.1.329-335.2005
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
19797
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:31
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Scientific Publication
Fate of predator and prey proteins during growth of Bdellovibrio bacteriovorus on Escherichia coli and Pseudomonas syringae prey
187
Barel, G., Dept. of Plant Pathol./Microbiol., Fac. Agric., Food/Environ. Qual. S., Hebrew University of Jerusalem, Rehovot, Israel
Sirota, A., Dept. of Genomics and Bioinformatics, Agricultural Research Organization, Bet Dagan, Israel
Volpin, H., Dept. of Genomics and Bioinformatics, Agricultural Research Organization, Bet Dagan, Israel
Jurkevitch, E., Dept. of Plant Pathol./Microbiol., Fac. Agric., Food/Environ. Qual. S., Hebrew University of Jerusalem, Rehovot, Israel, Dept. of Plant Pathol./Microbiol., Fac. Agric., Food/Environ. Qual. S., Hebrew University of Jerusalem, P.O. Box 12, 76100 Rehovot, Israel
Fate of predator and prey proteins during growth of Bdellovibrio bacteriovorus on Escherichia coli and Pseudomonas syringae prey
A two-dimensional electrophoretic analysis of protein distribution followed by identification of selected proteins by mass spectrometry was performed on fresh bdellovibrio cultures containing attack phase cells of the predatory bacterium Bdellovibrio bacteriovorus strain 109J-1 and the remains of an Escherichia coli or a Pseudomonas syringae pv. tomato prey. Cleavage of the peptidoglycan-associated outer membrane proteins (OMPs) OmpA in E. coli and OprF in P. syringae occurred in both prey. The tryptic peptides obtained from the cleavage products of OmpA and OprF were all located within the 19-kDa pronase-resistant N-terminal parts of the corresponding proteins. The predator cell fraction was separated from the prey ghosts in fresh bdellovibrio cultures by centrifugation on a Percoll-sucrose cushion. Proteins from each fraction were separated by two-dimensional electrophoresis and identified by mass spectrometric analysis. As no prey OMP could be detected in the predator cell fraction, it was concluded that prey OMPs are not transferred to the predator, as had been suggested previously. However, a protein from the predator was found bound to ghost cell envelopes. This protein may correspond to a protein earlier suggested to be associated with the prey outer or cytoplasmic membranes. Along with recently described polypeptides from B. bacteriovorus strains 100 and 114, it forms a new family of putative outer membrane proteins.
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