TY - JOUR
T1 - The proteolysis adaptor, NblA, is essential for degradation of the core pigment of the cyanobacterial light-harvesting complex
AU - Sendersky, Eleonora
AU - Kozer, Noga
AU - Levi, Mali
AU - Moizik, Michael
AU - Garini, Yuval
AU - Shav-Tal, Yaron
AU - Schwarz, Rakefet
N1 - Publisher Copyright:
© 2015 The Authors. © 2015 John Wiley & Sons Ltd.
PY - 2015/9/1
Y1 - 2015/9/1
N2 - The cyanobacterial light-harvesting complex, the phycobilisome, is degraded under nutrient limitation, allowing the cell to adjust light absorbance to its metabolic capacity. This large light-harvesting antenna comprises a core complex of the pigment allophycocyanin, and rod-shaped pigment assemblies emanating from the core. NblA, a low-molecular-weight protein, is essential for degradation of the phycobilisome. NblA mutants exhibit high absorbance of rod pigments under conditions that generally elicit phycobilisome degradation, implicating NblA in degradation of these pigments. However, the vast abundance of rod pigments and the substantial overlap between the absorbance spectra of rod and core pigments has made it difficult to directly associate NblA with proteolysis of the phycobilisome core. Furthermore, lack of allophycocyanin degradation in an NblA mutant may reflect a requirement for rod degradation preceding core degradation, and does not prove direct involvement of NblA in proteolysis of the core pigment. Therefore, in this study, we used a mutant lacking phycocyanin, the rod pigment of Synechococcus elongatusPCC7942, to examine whether NblA is required for allophycocyanin degradation. We demonstrate that NblA is essential for degradation of the core complex of the phycobilisome. Furthermore, fluorescence lifetime imaging microscopy provided in situ evidence for the interaction of NblA with allophycocyanin, and indicated that NblA interacts with allophycocyanin complexes that are associated with the photosynthetic membranes. Based on these data, as well as previous observations indicating interaction of NblA with phycobilisomes attached to the photosynthetic membranes, we suggest a model for sequential phycobilisome disassembly by NblA. Significance Statement Degradation of the light harvesting antenna complex is important during nutrient limitation. The detailed mechanism of proteolysis and the mode of disassembly of this complex are unclear. We show that the adaptor protein NblA is required for degradation of the core complex of the cyanobacterial light harvesting antennae and propose a role for NblA in sequential disassembly of the complex, thereby describing a novel function for NblA.
AB - The cyanobacterial light-harvesting complex, the phycobilisome, is degraded under nutrient limitation, allowing the cell to adjust light absorbance to its metabolic capacity. This large light-harvesting antenna comprises a core complex of the pigment allophycocyanin, and rod-shaped pigment assemblies emanating from the core. NblA, a low-molecular-weight protein, is essential for degradation of the phycobilisome. NblA mutants exhibit high absorbance of rod pigments under conditions that generally elicit phycobilisome degradation, implicating NblA in degradation of these pigments. However, the vast abundance of rod pigments and the substantial overlap between the absorbance spectra of rod and core pigments has made it difficult to directly associate NblA with proteolysis of the phycobilisome core. Furthermore, lack of allophycocyanin degradation in an NblA mutant may reflect a requirement for rod degradation preceding core degradation, and does not prove direct involvement of NblA in proteolysis of the core pigment. Therefore, in this study, we used a mutant lacking phycocyanin, the rod pigment of Synechococcus elongatusPCC7942, to examine whether NblA is required for allophycocyanin degradation. We demonstrate that NblA is essential for degradation of the core complex of the phycobilisome. Furthermore, fluorescence lifetime imaging microscopy provided in situ evidence for the interaction of NblA with allophycocyanin, and indicated that NblA interacts with allophycocyanin complexes that are associated with the photosynthetic membranes. Based on these data, as well as previous observations indicating interaction of NblA with phycobilisomes attached to the photosynthetic membranes, we suggest a model for sequential phycobilisome disassembly by NblA. Significance Statement Degradation of the light harvesting antenna complex is important during nutrient limitation. The detailed mechanism of proteolysis and the mode of disassembly of this complex are unclear. We show that the adaptor protein NblA is required for degradation of the core complex of the cyanobacterial light harvesting antennae and propose a role for NblA in sequential disassembly of the complex, thereby describing a novel function for NblA.
KW - Synechococcus elongatusPCC 7942
KW - adaptor
KW - allophycocyanin
KW - disassembly
KW - phycobilisome
KW - phycocyanin
KW - proteolysis
UR - http://www.scopus.com/inward/record.url?scp=84940187051&partnerID=8YFLogxK
U2 - 10.1111/tpj.12931
DO - 10.1111/tpj.12931
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C2 - 26173720
SN - 0960-7412
VL - 83
SP - 845
EP - 852
JO - Plant Journal
JF - Plant Journal
IS - 5
ER -