Limited proteolysis as a powerful tool for probing flexible oligopeptide portions among different classes of glutathione transferases

Marzia Nuccetelli; Cristina Evangelisti; Concetta Capo; Raffaele Petruzzelli; Michael W. Parker; Philip Board; Anna Maria Caccuri; Giorgio Federici; Giorgio Ricci; Mario Lo Bello

Limited proteolysis as a powerful tool for probing flexible oligopeptide portions among different classes of glutathione transferases

Marzia Nuccetelli, Cristina Evangelisti, Concetta Capo, Raffaele Petruzzelli, Michael W. Parker, Philip Board, Anna Maria Caccuri, Giorgio Federici, Giorgio Ricci, Mario Lo Bello^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

We have probed possible flexible regions of different GSTs by limited proteolysis experiments. The results indicate that each isoenzyme is inactivated by trypsin and protected against this proteolytic attack by glutathione (GSH). Unlike the results previously obtained with glutathione transferases (GST) GST P1-1, the region most susceptible to the cleavage and responsible for the loss of enzymatic activity in GST A1-1 is located at C-terminus (helix 9) whilst GST M2-2 does not show any primary cleavage site. These findings indicate that helix 2 of GST P1-1 and helix 9 of GST A1-1 may perform a class-specific role.

Original language	English
Pages (from-to)	49-50
Number of pages	2
Journal	Chemico-Biological Interactions
Volume	133
Issue number	1-3
Publication status	Published - 28 Feb 2001

Cite this

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title = "Limited proteolysis as a powerful tool for probing flexible oligopeptide portions among different classes of glutathione transferases",

abstract = "We have probed possible flexible regions of different GSTs by limited proteolysis experiments. The results indicate that each isoenzyme is inactivated by trypsin and protected against this proteolytic attack by glutathione (GSH). Unlike the results previously obtained with glutathione transferases (GST) GST P1-1, the region most susceptible to the cleavage and responsible for the loss of enzymatic activity in GST A1-1 is located at C-terminus (helix 9) whilst GST M2-2 does not show any primary cleavage site. These findings indicate that helix 2 of GST P1-1 and helix 9 of GST A1-1 may perform a class-specific role.",

keywords = "Enzymatic activity, Flexibility, Glutathione transferase, Limited proteolysis",

author = "Marzia Nuccetelli and Cristina Evangelisti and Concetta Capo and Raffaele Petruzzelli and Parker, {Michael W.} and Philip Board and Caccuri, {Anna Maria} and Giorgio Federici and Giorgio Ricci and {Lo Bello}, Mario",

year = "2001",

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day = "28",

language = "English",

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journal = "Chemico-Biological Interactions",

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T1 - Limited proteolysis as a powerful tool for probing flexible oligopeptide portions among different classes of glutathione transferases

AU - Nuccetelli, Marzia

AU - Evangelisti, Cristina

AU - Capo, Concetta

AU - Petruzzelli, Raffaele

AU - Parker, Michael W.

AU - Board, Philip

AU - Caccuri, Anna Maria

AU - Federici, Giorgio

AU - Ricci, Giorgio

AU - Lo Bello, Mario

PY - 2001/2/28

Y1 - 2001/2/28

N2 - We have probed possible flexible regions of different GSTs by limited proteolysis experiments. The results indicate that each isoenzyme is inactivated by trypsin and protected against this proteolytic attack by glutathione (GSH). Unlike the results previously obtained with glutathione transferases (GST) GST P1-1, the region most susceptible to the cleavage and responsible for the loss of enzymatic activity in GST A1-1 is located at C-terminus (helix 9) whilst GST M2-2 does not show any primary cleavage site. These findings indicate that helix 2 of GST P1-1 and helix 9 of GST A1-1 may perform a class-specific role.

AB - We have probed possible flexible regions of different GSTs by limited proteolysis experiments. The results indicate that each isoenzyme is inactivated by trypsin and protected against this proteolytic attack by glutathione (GSH). Unlike the results previously obtained with glutathione transferases (GST) GST P1-1, the region most susceptible to the cleavage and responsible for the loss of enzymatic activity in GST A1-1 is located at C-terminus (helix 9) whilst GST M2-2 does not show any primary cleavage site. These findings indicate that helix 2 of GST P1-1 and helix 9 of GST A1-1 may perform a class-specific role.

KW - Enzymatic activity

KW - Flexibility

KW - Glutathione transferase

KW - Limited proteolysis

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M3 - Article

SN - 0009-2797

VL - 133

SP - 49

EP - 50

JO - Chemico-Biological Interactions

JF - Chemico-Biological Interactions

IS - 1-3

ER -

Limited proteolysis as a powerful tool for probing flexible oligopeptide portions among different classes of glutathione transferases

Abstract

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