PMID- 12787025
OWN - NLM
STAT- MEDLINE
DCOM- 20030820
LR  - 20220309
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 270
IP  - 12
DP  - 2003 Jun
TI  - AtCYS1, a cystatin from Arabidopsis thaliana, suppresses hypersensitive cell 
      death.
PG  - 2593-604
AB  - In plants, cysteine protease inhibitors are involved in the regulation of protein 
      turnover and play an important role in resistance against insects and pathogens. 
      AtCYS1 from Arabidopsis thaliana encodes a protein of 102 amino acids that 
      contains the conserved motif of cysteine protease inhibitors belonging to the 
      cystatin superfamily (Gln-Val-Val-Ala-Gly). Recombinant A. thaliana cystatin-1 
      (AtCYS1) was expressed in Escherichia coli and purified. AtCYS1 inhibits the 
      catalytic activity of papain (Kd = 4.0 x 10-2 micro m, at pH 7.0 and 25 degrees 
      C), generally taken as a molecular model of cysteine proteases. The molecular 
      bases for papain inhibition by AtCYS1 have been analysed taking into account the 
      three-dimensional structure of the papain-stefin B complex. AtCYS1 is 
      constitutively expressed in roots and in developing siliques of A. thaliana. In 
      leaves, AtCYS1 is strongly induced by wounding, by challenge with avirulent 
      pathogens and by nitric oxide (NO). The overexpression of AtCYS1 blocks cell 
      death activated by either avirulent pathogens or by oxidative and nitrosative 
      stress in both A. thaliana suspension cultured cells and in transgenic tobacco 
      plants. The suppression of the NO-mediated cell death in plants overexpressing 
      AtCYS1 provides the evidence that NO is not cytotoxic for the plant, indicating 
      that NO functions as cell death trigger through the stimulation of an active 
      process, in which cysteine proteases and theirs proteinaceous inhibitors appear 
      to play a crucial role.
FAU - Belenghi, Beatrice
AU  - Belenghi B
AD  - Dipartimento Scientifico e Tecnologico, Universita degli Studi di Verona, Verona, 
      Italy.
FAU - Acconcia, Filippo
AU  - Acconcia F
FAU - Trovato, Maurizio
AU  - Trovato M
FAU - Perazzolli, Michele
AU  - Perazzolli M
FAU - Bocedi, Alessio
AU  - Bocedi A
FAU - Polticelli, Fabio
AU  - Polticelli F
FAU - Ascenzi, Paolo
AU  - Ascenzi P
FAU - Delledonne, Massimo
AU  - Delledonne M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (Cystatins)
RN  - 0 (Cysteine Proteinase Inhibitors)
RN  - 0 (DNA Primers)
RN  - 0 (Recombinant Proteins)
RN  - EC 3.4.22.2 (Papain)
SB  - IM
MH  - Amino Acid Sequence
MH  - Arabidopsis/*cytology/*physiology
MH  - Arabidopsis Proteins/*chemistry/metabolism
MH  - Base Sequence
MH  - Cell Death
MH  - Cells, Cultured
MH  - Cloning, Molecular
MH  - Conserved Sequence
MH  - Cystatins/*chemistry/metabolism
MH  - Cysteine Proteinase Inhibitors/chemistry/metabolism
MH  - DNA Primers
MH  - Escherichia coli/genetics
MH  - Humans
MH  - Molecular Sequence Data
MH  - Papain/antagonists & inhibitors
MH  - Polymerase Chain Reaction
MH  - Protein Conformation
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
EDAT- 2003/06/06 05:00
MHDA- 2003/08/21 05:00
CRDT- 2003/06/06 05:00
PHST- 2003/06/06 05:00 [pubmed]
PHST- 2003/08/21 05:00 [medline]
PHST- 2003/06/06 05:00 [entrez]
AID - 3630 [pii]
AID - 10.1046/j.1432-1033.2003.03630.x [doi]
PST - ppublish
SO  - Eur J Biochem. 2003 Jun;270(12):2593-604. doi: 10.1046/j.1432-1033.2003.03630.x.