C1A cysteine protease–cystatin interactions in leaf senescence
Author(s) -
Mercedes DíazMendoza,
Blanca VelascoArroyo,
Pablo GonzálezMelendi,
Manuel Martínez,
Isabel Dı́az
Publication year - 2014
Publication title -
journal of experimental botany
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 2.616
H-Index - 242
eISSN - 1460-2431
pISSN - 0022-0957
DOI - 10.1093/jxb/eru043
Subject(s) - proteases , proteolysis , cystatin , cysteine protease , cathepsin , senescence , biochemistry , protease , cysteine , biology , microbiology and biotechnology , enzyme , cystatin c , renal function
Senescence-associated proteolysis in plants is a crucial process to relocalize nutrients from leaves to growing or storage tissues. The massive net degradation of proteins involves broad metabolic networks, different subcellular compartments, and several types of proteases and regulators. C1A cysteine proteases, grouped as cathepsin L-, B-, H-, and F-like according to their gene structures and phylogenetic relationships, are the most abundant enzymes responsible for the proteolytic activity during leaf senescence. Besides, cystatins as specific modulators of C1A peptidase activities exert a complex regulatory role in this physiological process. This overview article covers the most recent information on C1A proteases in leaf senescence in different plant species. Particularly, it is focussed on barley, as the unique species where the whole gene family members of C1A cysteine proteases and cystatins have been analysed.
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