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פותח על ידי קלירמאש פתרונות בע"מ -
The Escherichia coli adenylyl cyclase complex: Requirement of PTS proteins for stimulation by nucleotides
Year:
1995
Source of publication :
Biochemistry (source )
Authors :
גולופ, נתן
;
.
Volume :
34
Co-Authors:
Peterkofsky, A., Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, Bethesda, MD 20892, United States, National Institutes of Health, Building 36, Bethesda, MD 20892, United States
Seok, Y.-J., Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, Bethesda, MD 20892, United States
Amin, N., Laboratory of Neurochemistry, National Institute of Neurological Diseases and Stroke, Bethesda, MD 20892, United States
Thapar, R., Department of Biochemistry, University of Washington, Seattle, WA 98195, United States
Lee, S.Y., Department of Biochemistry, University of Washington, Seattle, WA 98195, United States
Klevit, R.E., Department of Biochemistry, University of Washington, Seattle, WA 98195, United States
Waygood, E.B., Department of Biochemistry, University of Saskatchewan, Saskatoon, Sask. S7N 0W0, Canada
Anderson, J.W., Department of Biochemistry, University of Saskatchewan, Saskatoon, Sask. S7N 0W0, Canada
Gruschus, J., Laboratory of Biophysical Chemistry, National Heart, Lung and Blood Institute, Bethesda, MD 20892, United States
Huq, H., Laboratory of Biophysical Chemistry, National Heart, Lung and Blood Institute, Bethesda, MD 20892, United States
Gollop, N., Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, Bethesda, MD 20892, United States, Volcani Center, Bet-Dagen 50250, Israel
Facilitators :
From page:
8950
To page:
8959
(
Total pages:
10
)
Abstract:
GTP, as well as other nucleoside triphosphates, stimulates the activity of Escherichia coli adenylyl cyclase in permeable cells; the stimulatory effect is lost when the cells are disrupted by passage through a French pressure cell. These data suggested that the allosteric regulation by GTP of adenylyl cyclase activity requires an interaction of the enzyme with other protein factors. Strains deleted for genes encoding proteins of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) failed to show an activity stimulation by GTP. With a view to localizing the site of interaction of GTP with the adenylyl cyclase complex, a variety of studies using purified PTS proteins were performed using the photoaffinity labeling reagent, 8-azidoGTP. These studies showed that 8-azidoGTP bound specifically to HPr. A species specificity study showed that the photoaffinity reagent labeled E. coli HPr but not HPr proteins from Mycoplasma capricolum or Bacillus subtilis. A variety of site-directed mutations of E. coli HPr were evaluated for interaction with GTP by photoaffinity labeling as well as by nuclear magnetic resonance; the results of these studies indicate that the lysine residues at positions 24 and 27, serine-46, the threonine at position 36, and the aspartate at position 69 are important for the binding of GTP to HPr. Molecular modeling has been used to formulate a model for the binding of GTP to HPr involving electrostatic interaction of the phosphate groups of the nucleotide with the side chains of lysine residues 27 and 45 and serine-43, interaction of the sugar with serine-46, and interaction of the base with lysine-24. From these data, it is hypothesized that the binding of GTP to HPr is required for the GTP-dependent stimulation of the activity of the adenylyl cyclase complex. © 1995 American Chemical Society.
Note:
Related Files :
Base Sequence
Binding Sites
enzyme binding
Models, Biological
Models, Molecular
Molecular Sequence Data
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
20206
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:34
Scientific Publication
The Escherichia coli adenylyl cyclase complex: Requirement of PTS proteins for stimulation by nucleotides
34
Peterkofsky, A., Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, Bethesda, MD 20892, United States, National Institutes of Health, Building 36, Bethesda, MD 20892, United States
Seok, Y.-J., Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, Bethesda, MD 20892, United States
Amin, N., Laboratory of Neurochemistry, National Institute of Neurological Diseases and Stroke, Bethesda, MD 20892, United States
Thapar, R., Department of Biochemistry, University of Washington, Seattle, WA 98195, United States
Lee, S.Y., Department of Biochemistry, University of Washington, Seattle, WA 98195, United States
Klevit, R.E., Department of Biochemistry, University of Washington, Seattle, WA 98195, United States
Waygood, E.B., Department of Biochemistry, University of Saskatchewan, Saskatoon, Sask. S7N 0W0, Canada
Anderson, J.W., Department of Biochemistry, University of Saskatchewan, Saskatoon, Sask. S7N 0W0, Canada
Gruschus, J., Laboratory of Biophysical Chemistry, National Heart, Lung and Blood Institute, Bethesda, MD 20892, United States
Huq, H., Laboratory of Biophysical Chemistry, National Heart, Lung and Blood Institute, Bethesda, MD 20892, United States
Gollop, N., Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, Bethesda, MD 20892, United States, Volcani Center, Bet-Dagen 50250, Israel
The Escherichia coli adenylyl cyclase complex: Requirement of PTS proteins for stimulation by nucleotides
GTP, as well as other nucleoside triphosphates, stimulates the activity of Escherichia coli adenylyl cyclase in permeable cells; the stimulatory effect is lost when the cells are disrupted by passage through a French pressure cell. These data suggested that the allosteric regulation by GTP of adenylyl cyclase activity requires an interaction of the enzyme with other protein factors. Strains deleted for genes encoding proteins of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) failed to show an activity stimulation by GTP. With a view to localizing the site of interaction of GTP with the adenylyl cyclase complex, a variety of studies using purified PTS proteins were performed using the photoaffinity labeling reagent, 8-azidoGTP. These studies showed that 8-azidoGTP bound specifically to HPr. A species specificity study showed that the photoaffinity reagent labeled E. coli HPr but not HPr proteins from Mycoplasma capricolum or Bacillus subtilis. A variety of site-directed mutations of E. coli HPr were evaluated for interaction with GTP by photoaffinity labeling as well as by nuclear magnetic resonance; the results of these studies indicate that the lysine residues at positions 24 and 27, serine-46, the threonine at position 36, and the aspartate at position 69 are important for the binding of GTP to HPr. Molecular modeling has been used to formulate a model for the binding of GTP to HPr involving electrostatic interaction of the phosphate groups of the nucleotide with the side chains of lysine residues 27 and 45 and serine-43, interaction of the sugar with serine-46, and interaction of the base with lysine-24. From these data, it is hypothesized that the binding of GTP to HPr is required for the GTP-dependent stimulation of the activity of the adenylyl cyclase complex. © 1995 American Chemical Society.
Scientific Publication
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