Published January 11, 2022 | Version v1
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Proteolytic cleavage of Arabidopsis thaliana phosphoenolpyruvate carboxykinase-1 modifies its allosteric regulation

  • 1. National Scientific and Technical Research Council

Description

Phosphoenolpyruvate carboxykinase (PEPCK) plays a crucial role in gluconeogenesis. In this work, we analyze the proteolysis of Arabidopsis thaliana PEPCK1 (AthPEPCK1) in germinating seedlings. We found that the amount of AthPEPCK1 protein peaks at 24-48 hours post-imbibition. Concomitantly, we observed shorter versions of AthPEPCK1, putatively generated by metacaspase-9 (AthMC9). To study the impact of AthMC9 cleavage on the kinetic and regulatory properties of AthPEPCK1, we produced truncated mutants based on the reported AthMC9 cleavage sites. The Δ19 and Δ101 truncated mutants of AthPEPCK1 showed similar kinetic parameters and the same quaternary structure than the WT. However, activation by malate and inhibition by glucose 6-phosphate were abolished in the Δ101 mutant. We propose that proteolysis of AthPEPCK1 in germinating seedlings operates as a mechanism to adapt the sensitivity to allosteric regulation during the sink-to-source transition.

Notes

Funding provided by: Agencia Nacional de Promoción Científica y Tecnológica
Crossref Funder Registry ID: http://dx.doi.org/10.13039/501100003074
Award Number: PICT-2017-1515

Funding provided by: Agencia Nacional de Promoción Científica y Tecnológica
Crossref Funder Registry ID: http://dx.doi.org/10.13039/501100003074
Award Number: PICT-2018-00929

Funding provided by: Agencia Nacional de Promoción Científica y Tecnológica
Crossref Funder Registry ID: http://dx.doi.org/10.13039/501100003074
Award Number: PICT-2018-00865

Funding provided by: Max-Planck-Gesellschaft
Crossref Funder Registry ID: http://dx.doi.org/10.13039/501100004189
Award Number: Partner Group for Plant Biochemistry

Funding provided by: Universidad Nacional del Litoral
Crossref Funder Registry ID: http://dx.doi.org/10.13039/501100005746
Award Number: CAI+D

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Is cited by
10.1093/jxb/eraa583 (DOI)