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Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria
by
Steglich, Claudia
, Fahrner, Matthias
, Frankenberg-Dinkel, Nicole
, Krauspe, Vanessa
, Spät, Philipp
, Schilling, Oliver
, Hess, Wolfgang R.
, Maček, Boris
in
Biological Sciences
/ Plant Biology
2021
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Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria
by
Steglich, Claudia
, Fahrner, Matthias
, Frankenberg-Dinkel, Nicole
, Krauspe, Vanessa
, Spät, Philipp
, Schilling, Oliver
, Hess, Wolfgang R.
, Maček, Boris
in
Biological Sciences
/ Plant Biology
2021
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Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria
by
Steglich, Claudia
, Fahrner, Matthias
, Frankenberg-Dinkel, Nicole
, Krauspe, Vanessa
, Spät, Philipp
, Schilling, Oliver
, Hess, Wolfgang R.
, Maček, Boris
in
Biological Sciences
/ Plant Biology
2021
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Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria
Journal Article
Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria
2021
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Overview
Phycobilisomes are the major pigment–protein antenna complexes that perform photosynthetic light harvesting in cyanobacteria, rhodophyte, and glaucophyte algae. Up to 50% of the cellular nitrogen can be stored in their giant structures. Accordingly, upon nitrogen depletion, phycobilisomes are rapidly degraded following an intricate genetic program. Here, we describe the role of NblD, a cysteine-rich, small protein in this process in cyanobacteria. Deletion of the nblD gene in the cyanobacterium Synechocystis sp. PCC 6803 prevented the degradation of phycobilisomes, leading to a nonbleaching (nbl) phenotype, which could be complemented by a plasmid-localized gene copy. Competitive growth experiments between the ΔnblD and the wild-type strain provided direct evidence for the physiological importance of NblD under nitrogen-limited conditions. Ectopic expression of NblD under nitrogen-replete conditions showed no effect, in contrast to the unrelated proteolysis adaptors NblA1 and NblA2, which can trigger phycobilisome degradation. Transcriptome analysis indicated increased nblA1/2 transcript levels in the ΔnblD strain during nitrogen starvation, implying that NblD does not act as a transcriptional (co) regulator. However, immunoprecipitation and far-western experiments identified the chromophorylated (holo form) of the phycocyanin β-subunit (CpcB) as its target, while apo-CpcB was not bound. The addition of recombinant NblD to isolated phycobilisomes caused a reduction in phycocyanin absorbance and a broadening and shifting of the peak to lower wavelengths, indicating the occurrence of structural changes. These data demonstrate that NblD plays a crucial role in the coordinated dismantling of phycobilisomes and add it as a factor to the genetically programmed response to nitrogen starvation.
Publisher
National Academy of Sciences
Subject
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