Dr. Song, Hyun-kyu: provide the coordinates of ClpS1 (PDB 7d34)2024-12-202024-12-202021-06-14Aguilar Lucero, D., Cantoia, A., Sánchez López, C., Binolfi, A., Mogk, A., Ceccarelli, E.A. and Rosano, G.L. (2021). Structural features of the plant N-recognin ClpS1 and sequence determinants in its targets that govern substrate selection. FEBS Letters, 595(11), 1525-1541. https://doi.org/10.1002/1873-3468.140810014-5793https://hdl.handle.net/2133/28503In the N-degron pathway of protein degradation of Escherichia coli, the N-recognin ClpS identifies substrates bearing N-terminal phenylalanine, tyrosine, tryptophan, or leucine and delivers them to the caseinolytic protease (Clp). Chloroplasts contain the Clp system, but whether chloroplastic ClpS1 adheres to the same constraints is unknown. Moreover, the structural underpinnings of substrate recognition are not completely defined. We show that ClpS1 recognizes canonical residues of the E. coli N-degron pathway. The residue in second position influences recognition (especially in N-terminal ends starting with leucine). N-terminal acetylation abrogates recognition. ClpF, a ClpS1-interacting partner, does not alter its specificity. Substrate binding provokes local remodeling of residues in the substrate-binding cavity of ClpS1. Our work strongly supports the existence of a chloroplastic N-degron pathway.1-17enopenAccessAdaptorArabidopsis thalianaChloroplastN-degron pathwayClpS1ProteolysisarticuloAguilar Lucero, Dianela AilinCantoia, AlejoSánchez López, CarolinaBinolfi, AndrésMogk, AxelCeccarelli, Eduardo AugustoRosano, Germán L.Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y FarmacéuticasAttribution-NonCommercial-NoDerivatives 4.0 International1873-3468