Oxidation of proline from the cyclin-binding motif in maize CDKA;1 results in lower affinity with its cyclin regulatory subunit

ANDREA AE MENDEZ; LILIANA B PENA; LUCRECIA M CURTO; MARISA M FERNANDEZ; EMILIO L MALCHIODI; SARA M GARZA-AGUILAR; JORGE M VAZQUEZ RAMOS

PHYTOCHEMISTRY

PERGAMON-ELSEVIER SCIENCE LTD

Lugar: Amsterdam; Año: 2019

0031-9422

Cyclin dependent kinase A; 1 (CDKA; 1) is essential in G1/S transition of cell cycle and its oxidation has beenimplicated in cell cycle arrest during plant abiotic stress. In the present study, an evaluation at the molecularlevel was performed to find possible sites of protein oxidative modifications. In vivo studies demonstrated thatcarbonylation of maize CDKA,1 is associated with a decrease in complex formation with maize cyclin D (CycD).Control and in vitro oxidized recombinant CDKA; 1 were sequenced by mass spectrometry. Proline at the PSTAIREcyclin-binding motif was identified as the most susceptible oxidation site by comparative analysis of the resultedpeptides. The specific interaction between CDKA; 1 and CycD6; 1, measured by surface plasmon resonance (SPR),demonstrated that the affinity and the kinetic of the interaction depended on the reduced-oxidized state of theCDKA; 1. CDKA; 1 protein oxidative modification would be in part responsible for affecting cell cycle progression,and thus producing plant growth inhibition under oxidative stress.