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Abstract:

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.

Registro:

Documento: Artículo
Título:Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action
Autor:Murray, P.F.; Passeron, S.
Filiación:Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, 4° Piso, Pabellón II, Buenos Aires, 1428, Argentina
Palabras clave: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
Año:1994
Volumen:18
Número:4
Página de inicio:320
Página de fin:329
DOI: http://dx.doi.org/10.1016/S0147-5975(06)80005-8
Título revista:Experimental Mycology
Título revista abreviado:Exp. Mycol.
ISSN:01475975
CAS:aminopeptidase, 9031-94-1; cyclic AMP dependent protein kinase; leucine, 61-90-5, 7005-03-0; serine, 56-45-1, 6898-95-9; subtilisin, 9014-01-1; tritium, 10028-17-8
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01475975_v18_n4_p320_Murray

Referencias:

  • Arbesú, M.J., Gascon, S., Suarez-Rendueles, P., Isolation and characterization of Schizosaccharomyces pombe mutants lacking aminopeptidase activity (1991) Yeast, 7, pp. 525-531
  • Benore-Parsons, M., Seidah, N.G., Wennogle, L.P., Substrate phosphorylation can inhibit proteolysis by trypsin-like enzymes (1989) Arch. Biochem. Biophys., 272, pp. 274-280
  • Botbol, V., Scornik, O.A., Role of bestatin-sensitive exopeptidases in the intracellular degradation of hepatic proteins (1989) J. Biol. Chem., 264, pp. 13504-13509
  • Bradford, M.M., A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254
  • Bramucci, M., Miano, A., Amici, D., Epidermal inhibitory pentapeptide phosphorylated in vitro by calf thymus protein kinase NII is protected from serum enzyme hydrolysis (1992) Biochem. Biophys. Res. Commun., 183, pp. 474-480
  • Chen, M., Stracher, A., In situ phosphorylation of platelet actin-binding protein by cAMPdependent protein kinase stabilizes it against proteolysis by calpain (1989) J. Biol. Chem., 264, pp. 14282-14289
  • Edman, P., Method for the determination of the amino acid sequence in peptides (1950) Acta Chemica Scandinavica, 4, pp. 283-293
  • Ekman, P., Hermansson, U., Bergström, G., Engström, L., Rapid proteolytic removal of phosphopeptides and phosphorylatable sites from proteins in rat liver cell sap (1978) FEBS Lett., 86, pp. 250-254
  • Fernandez Murray, P., Silberstein, S., Cantore, M.L., Passeron, S., A radioactive method for the measurement of trypsin and trypsinlike activities (1989) Anal. Biochem., 179, pp. 56-59
  • Fernandez Murray, P., Samela, A., Passeron, S., Purification and characterization of an aminopeptidase from the fungus Saccobolus platensis (1992) Exp. Mycol., 16, pp. 279-290
  • Garland, D., Nimmo, H.G., A comparison of the phosphorylated and unphosphorylated forms of isocitrate dehydrogenase from Escherichia coli ML308 (1984) FEBS Lett., 165, pp. 259-264
  • Green, G.R., Lee, H., Poccia, D.L., Phosphorylation weakens DNA binding by peptides containing multiple “SPKK” sequences (1993) J. Biol. Chem., 268, pp. 11247-11255
  • Hilt, W., Wolf, D.H., Stress-induced proteolysis in yeast (1992) Mol. Microbiol., 6, pp. 2437-2442
  • Jones, E.W., Three proteolytic systems in the yeast. Saccharomyces cerevisiae (1991) J. Biol. Chem., 266, pp. 7963-7966
  • Light, A., Leucine aminopeptidase in sequence determination of peptides (1972) Methods Enzymol, 25, pp. 253-262
  • Madapallimattam, G., Bennick, A., Phosphopeptides derived from human salivary acidic proline-rich proteins (1990) Biochem. J., 270, pp. 297-304
  • Minagawa, E., Kaminogawa, S., Matsuzawa, H., Ohta, T., Yamauchi, K., Isolation and characterization of a thermostable aminopeptidase (Aminopeptidase T) from Thermus aquaticus YT-1, an extremely thermophilic bacterium (1988) Agricultural and Biological Chemistry, 52, pp. 1755-1763
  • Orlowski, M., Michaud, C., Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolytic activity (1989) Biochemistry, 28, pp. 9270-9278
  • Reimann, E.M., Beham, R.A., Catalytic subunit of cAMP-dependent protein kinase (1983) Methods Enzymol., 99, pp. 51-55
  • Roskoski, R., Jr, Assays of protein kinase (1983) Methods Enzymol., 99, pp. 3-6
  • Stadtman, E.R., Covalent modification reactions are marking steps in protein turnover (1990) Biochemistry, 29, pp. 6323-6331
  • Wolf, D.H., Proteases as biological regulators (1992) Experientia, 48, pp. 117-118

Citas:

---------- APA ----------
Murray, P.F. & Passeron, S. (1994) . Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action. Experimental Mycology, 18(4), 320-329.
http://dx.doi.org/10.1016/S0147-5975(06)80005-8
---------- CHICAGO ----------
Murray, P.F., Passeron, S. "Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action" . Experimental Mycology 18, no. 4 (1994) : 320-329.
http://dx.doi.org/10.1016/S0147-5975(06)80005-8
---------- MLA ----------
Murray, P.F., Passeron, S. "Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action" . Experimental Mycology, vol. 18, no. 4, 1994, pp. 320-329.
http://dx.doi.org/10.1016/S0147-5975(06)80005-8
---------- VANCOUVER ----------
Murray, P.F., Passeron, S. Phosphorylated peptides can limit Saccobolus platensis aminopeptidase action. Exp. Mycol. 1994;18(4):320-329.
http://dx.doi.org/10.1016/S0147-5975(06)80005-8