Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action
The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by purified aminopeptidase from Saccobolus platensis was investigated using the model heptapeptide L-R-R-A-S-L-G. Phosphorylation of serine greatly altered the action of peptidase producing a fragment, A-S(P)-L-G,...
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1994
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v18_n4_p320_Murray http://hdl.handle.net/20.500.12110/paper_01475975_v18_n4_p320_Murray |
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paper:paper_01475975_v18_n4_p320_Murray2023-06-08T15:12:46Z Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action aminopeptidase cyclic AMP-dependent protein kinase dithiothreitol DTT kemptide L-R-R-A-S-L-G peptide processing phosphopeptides phosphorylation PK A proteolysis aminopeptidase cyclic AMP dependent protein kinase heptapeptide leucine serine subtilisin tritium article cytosol enzyme activity fungus gel filtration nonhuman priority journal protein degradation protein phosphorylation Fungi Saccobolus Tritium The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by purified aminopeptidase from Saccobolus platensis was investigated using the model heptapeptide L-R-R-A-S-L-G. Phosphorylation of serine greatly altered the action of peptidase producing a fragment, A-S(P)-L-G, insensitive to further attack by the peptidase. The action of peptidase was tested on peptides generated by subtilisin digestion of fungal cytosolic proteins labeled in vivo with [3H]leucine and phosphorylated in vitro with the catalytic subunit of cyclic AMP-dependent protein kinase. Phosphopeptides were enriched by gel filtration through P-2 columns. After exhaustive exopeptidase degradation the peak of [32p]phosphopeptides remained mostly unchanged. Removal of phosphate with alkaline phosphatase prior to treatment with peptidase produced a 12% liberation of [3H]leucine. The results support the idea that phosphorylation influences final protein processing. © 1994, Academic Press, Inc.. All rights reserved. 1994 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v18_n4_p320_Murray http://hdl.handle.net/20.500.12110/paper_01475975_v18_n4_p320_Murray |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
aminopeptidase cyclic AMP-dependent protein kinase dithiothreitol DTT kemptide L-R-R-A-S-L-G peptide processing phosphopeptides phosphorylation PK A proteolysis aminopeptidase cyclic AMP dependent protein kinase heptapeptide leucine serine subtilisin tritium article cytosol enzyme activity fungus gel filtration nonhuman priority journal protein degradation protein phosphorylation Fungi Saccobolus Tritium |
| spellingShingle |
aminopeptidase cyclic AMP-dependent protein kinase dithiothreitol DTT kemptide L-R-R-A-S-L-G peptide processing phosphopeptides phosphorylation PK A proteolysis aminopeptidase cyclic AMP dependent protein kinase heptapeptide leucine serine subtilisin tritium article cytosol enzyme activity fungus gel filtration nonhuman priority journal protein degradation protein phosphorylation Fungi Saccobolus Tritium Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action |
| topic_facet |
aminopeptidase cyclic AMP-dependent protein kinase dithiothreitol DTT kemptide L-R-R-A-S-L-G peptide processing phosphopeptides phosphorylation PK A proteolysis aminopeptidase cyclic AMP dependent protein kinase heptapeptide leucine serine subtilisin tritium article cytosol enzyme activity fungus gel filtration nonhuman priority journal protein degradation protein phosphorylation Fungi Saccobolus Tritium |
| description |
The effect of substrate phosphorylation on the susceptibility to proteolytic cleavage by purified aminopeptidase from Saccobolus platensis was investigated using the model heptapeptide L-R-R-A-S-L-G. Phosphorylation of serine greatly altered the action of peptidase producing a fragment, A-S(P)-L-G, insensitive to further attack by the peptidase. The action of peptidase was tested on peptides generated by subtilisin digestion of fungal cytosolic proteins labeled in vivo with [3H]leucine and phosphorylated in vitro with the catalytic subunit of cyclic AMP-dependent protein kinase. Phosphopeptides were enriched by gel filtration through P-2 columns. After exhaustive exopeptidase degradation the peak of [32p]phosphopeptides remained mostly unchanged. Removal of phosphate with alkaline phosphatase prior to treatment with peptidase produced a 12% liberation of [3H]leucine. The results support the idea that phosphorylation influences final protein processing. © 1994, Academic Press, Inc.. All rights reserved. |
| title |
Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action |
| title_short |
Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action |
| title_full |
Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action |
| title_fullStr |
Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action |
| title_full_unstemmed |
Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action |
| title_sort |
phosphorylated peptides can limit saccobolus platensis aminopeptidase action |
| publishDate |
1994 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v18_n4_p320_Murray http://hdl.handle.net/20.500.12110/paper_01475975_v18_n4_p320_Murray |
| _version_ |
1768545137882824704 |