Senescence-associated degradation of chloroplast proteins inside and outside the organelle.
Leaf proteins, and in particular the photosynthetic proteins of plastids, are extensively degraded during senescence. Although this involves massive amounts of protein, the mechanisms responsible for chloroplast protein degradation are largely unknown. Degradation within the plastid itself is supported by the observation that chloroplasts contain active proteases, and that chloroplasts isolated from senescing leaves can cleave Rubisco to release partially digested fragments. It is less clear whether chloroplasts can complete Rubisco degradation. Chloroplastic proteases are likely involved in the breakdown of the D1 and LHCII proteins of photosystem II. Small senescence-associated vacuoles (SAVs) with high-proteolytic activity develop in senescing leaf cells, and there is evidence that SAVs contain chloroplast proteins. Thus, an extra-plastidic pathway involving SAVs might participate in the degradation of some chloroplast proteins. Plastidic and extra-plastidic pathways might cooperate in the degradation of chloroplast proteins, or they might represent alternative, redundant pathways for photosynthetic protein degradation.
Martínez
D E
DE
Instituto de Fisiología Vegetal, Universidad Nacional de La Plata, La Plata, Argentina.
Costa
M L
ML
Guiamet
J J
JJ
D001343:Autophagy / Q000502:physiology; D016922:Cellular Senescence; D002736:Chloroplasts / Q000378:metabolism*; D008954:Models, Biological; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism; D018515:Plant Leaves / Q000254:growth & development / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism; D014617:Vacuoles / Q000378:metabolism / Q000502:physiology
D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins; D012273:Ribulose-Bisphosphate Carboxylase