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Localisation and interactions of the Vipp1 protein in cyanobacteria

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  • Samantha J Bryan
  • Nigel J Burroughs
  • Dmitriy Shevela
  • Jianfeng Yu
  • Eva Rupprecht
  • Lu-Ning Liu
  • Giulia Mastroianni
  • Quan Xue
  • Isabel Llorente-Garcia
  • Mark Christian Leake
  • Lutz A Eichacker
  • Dirk Schneider
  • Peter J Nixon
  • Conrad W Mullineaux


Publication details

JournalMolecular Microbiology
DateE-pub ahead of print - 30 Oct 2014
DatePublished (current) - Dec 2014
Issue number5
Number of pages17
Pages (from-to)1179-1195
Early online date30/10/14
Original languageEnglish


The Vipp1 protein is essential in cyanobacteria and chloroplasts for the maintenance of photosynthetic function and thylakoid membrane architecture. To investigate its mode of action we generated strains of the cyanobacteria Synechocystis sp. PCC6803 and Synechococcus sp. PCC7942 in which Vipp1 was tagged with green fluorescent protein at the C-terminus and expressed from the native chromosomal locus. There was little perturbation of function. Live-cell fluorescence imaging shows dramatic relocalisation of Vipp1 under high light. Under low light, Vipp1 is predominantly dispersed in the cytoplasm with occasional concentrations at the outer periphery of the thylakoid membranes. High light induces Vipp1 coalescence into localised puncta within minutes, with net relocation of Vipp1 to the vicinity of the cytoplasmic membrane and the thylakoid membranes. Pull-downs and mass spectrometry identify an extensive collection of proteins that are directly or indirectly associated with Vipp1 only after high-light exposure. These include not only photosynthetic and stress-related proteins but also RNA-processing, translation and protein assembly factors. This suggests that the Vipp1 puncta could be involved in protein assembly. One possibility is that Vipp1 is involved in the formation of stress-induced localised protein assembly centres, enabling enhanced protein synthesis and delivery to membranes under stress conditions.

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© 2012 The Authors. This content is made available by the publisher under a Creative Commons CC-BY Licence

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