The Arabidopsis METACASPASE9 Degradome

被引:95
作者
Tsiatsiani, Liana [1 ,2 ,3 ,4 ]
Timmerman, Evy [3 ,4 ]
De Bock, Pieter-Jan [3 ,4 ]
Vercammen, Dominique [1 ,2 ]
Stael, Simon [1 ,2 ,3 ,4 ]
van de Cotte, Brigitte [1 ,2 ]
Staes, An [3 ,4 ]
Goethals, Marc [3 ,4 ]
Beunens, Tine [1 ,2 ]
Van Damme, Petra [3 ,4 ]
Gevaert, Kris [3 ,4 ]
Van Breusegem, Frank [1 ,2 ]
机构
[1] Univ Ghent VIB, Dept Plant Syst Biol, B-9052 Ghent, Belgium
[2] Univ Ghent, Dept Plant Biotechnol & Bioinformat, B-9052 Ghent, Belgium
[3] Univ Ghent VIB, Dept Med Prot Res, B-9000 Ghent, Belgium
[4] Univ Ghent, Dept Biochem, B-9000 Ghent, Belgium
关键词
PROGRAMMED CELL-DEATH; LEISHMANIA-MAJOR METACASPASE; PHOSPHOENOLPYRUVATE CARBOXYKINASE; TRYPANOSOMA-BRUCEI; PLANT PROTEASES; COORDINATE REGULATION; CYSTEINE PROTEASES; YEAST METACASPASE; IN-VIVO; PROTEIN;
D O I
10.1105/tpc.113.115287
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Metacaspases are distant relatives of the metazoan caspases, found in plants, fungi, and protists. However, in contrast with caspases, information about the physiological substrates of metacaspases is still scarce. By means of N-terminal combined fractional diagonal chromatography, the physiological substrates of METACASPASE9 (MC9; AT5G04200) were identified in young seedlings of Arabidopsis thaliana on the proteome-wide level, providing additional insight into MC9 cleavage specificity and revealing a previously unknown preference for acidic residues at the substrate prime site position P1'. The functionalities of the identified MC9 substrates hinted at metacaspase functions other than those related to cell death. These results allowed us to resolve the substrate specificity of MC9 in more detail and indicated that the activity of phosphoenolpyruvate carboxykinase 1 (AT4G37870), a key enzyme in gluconeogenesis, is enhanced upon MC9-dependent proteolysis.
引用
收藏
页码:2831 / 2847
页数:17
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