Energy Sensing versus 2-Oxoglutarate Dependent ATPase Switch in the Control of Synechococcus PII Interaction with Its Targets NAGK and PipX

PloS One
Jan Lüddecke, Karl Forchhammer

Abstract

PII proteins constitute a superfamily of highly conserved signaling devices, common in all domains of life. Through binding of the metabolites ATP, ADP and 2-oxoglutarate (2-OG), they undergo conformational changes which allow them to regulate a variety of target proteins including enzymes, transport proteins and transcription factors. But, in reverse, these target proteins also modulate the metabolite sensing properties of PII, as has been recently shown. We used this effect to refine our PII based Förster resonance energy transfer (FRET) sensor and amplify its sensitivity towards ADP. With this enhanced sensor setup we addressed the question whether the PII protein from the model organism Synechococcus elongatus autonomously switches into the ADP conformation through ATPase activity as proposed in a recently published model. The present study disproves ATPase activity as a relevant mechanism for the transition of PII into the ADP state. In the absence of 2-OG, only the ATP/ADP ratio and concentration of ADP directs the competitive interaction of PII with two targets, one of which preferentially binds PII in the ATP-state, the other in the ADP-state.

References

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Citations

Nov 4, 2015·The FEBS Journal·Karl Forchhammer, Jan Lüddecke
May 19, 2017·Journal of Experimental Botany·Aaron Kaplan
Feb 15, 2018·Environmental Microbiology·Javier EspinosaAsunción Contreras
May 8, 2018·Proceedings of the National Academy of Sciences of the United States of America·Khaled A SelimKarl Forchhammer
Aug 21, 2018·Environmental Microbiology Reports·Raquel CantosAsunción Contreras
Oct 16, 2018·Environmental Microbiology·Karl Forchhammer, Rakefet Schwarz
Jun 3, 2020·Life·Jose I LabellaAsunción Contreras
May 5, 2017·Scientific Reports·Jan LüddeckeKarl Forchhammer
Aug 10, 2017·Frontiers in Plant Science·Aurora ParlatiMaurizio Chiurazzi

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Methods Mentioned

BETA
FRET
surface plasmon resonance spectroscopy
protein
affinity purification

Software Mentioned

GraphPad Prism

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