期刊
PHYSIOLOGIA PLANTARUM
卷 145, 期 1, 页码 77-84出版社
WILEY-BLACKWELL
DOI: 10.1111/j.1399-3054.2011.01560.x
关键词
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资金
- Russian Foundation for Basic Research
- Russian Ministry of Education and Science [P334, 14.740.11.0168, 02.740.11.5145]
- Royal Society
- Scottish Government
Proteases with an aspartate cleavage specificity are known to contribute to programmed cell death (PCD) in animals and plants. In animal cells this proteolytic activity belongs to caspases, a well-characterized family of cysteine-dependent death proteases. Plants, however, lack caspase homologs and thus the origin of this type of proteolytic activity in planta was poorly understood. Here, we review recent data demonstrating that a plant serine-dependent protease, phytaspase, shares cleavage specificity and a role in PCD analogous to that of caspases. However, unlike caspases, regulation of phytaspase-mediated cleavage of intracellular target proteins appears to be attained not at the level of proenzyme processing/activation, which occurs, in the case of phytaspase, autocatalytically and constitutively. Rather, the mature phytaspase is excluded from healthy cells into the apoplast and is allowed to re-enter cells upon the induction of PCD. Thus, PCD-related proteases in animals and plants display both common features and important distinctions.
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