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

MENDEZ AE; PENA LILIANA B; CURTO, LUCRECIA M.; FERNANDEZ.MARISA M.; MALCHIODI, EMILIO L.; GARZA AGUILAR SM; VAZQUEZ-RAMOS JM; GALLEGO SM

PHYTOCHEMISTRY

PERGAMON-ELSEVIER SCIENCE LTD

Lugar: Amsterdam; Año: 2020

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 tofind possible sites of protein oxidative modifications.In vivostudies demonstrated thatcarbonylation of maize CDKA,1 is associated with a decrease in complex formation with maize cyclin D (CycD).Control andin vitrooxidized recombinant CDKA; 1 were sequenced by mass spectrometry. Proline at thePSTAIRE cyclin-binding motif was identified as the most susceptible oxidation site by comparative analysis ofthe resulted peptides. The specific interaction between CDKA; 1 and CycD6; 1, measured by surface plasmonresonance (SPR), demonstrated that the affinity and the kinetic of the interaction depended on the reduced-oxidized state of the CDKA; 1. CDKA; 1 protein oxidative modification would be in part responsible for affectingcell cycle progression, and thus producing plant growth inhibition under oxidative stres