Structural features of the plant N-recognin ClpS1 and sequence determinants in its targets that govern substrate selection

FEBS Letters

article

Dianela Aguilar Lucero¹  Alejo Cantoia¹  Carolina Sánchez-López¹  Andrés Binolfi¹  Axel Mogk³  Eduardo A. Ceccarelli¹  Germán L. Rosano¹ 

[1] CONICET, Facultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Biología Molecular y Celular de Rosario ,(IBR), Universidad Nacional de Rosario;Plataforma Argentina de Biología Estructural y Metabolómica ,(PLABEM);DKFZ-ZMBH Alliance, Zentrum für Molekulare Biologie der Universität Heidelberg

关键词: adaptor;    Arabidopsis thaliana;    chloroplast;    N-degron pathway;    proteolysis;   

DOI  :  10.1002/1873-3468.14081

来源: John Wiley & Sons Ltd.

【 摘 要 】

In 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.

【 授权许可】

Unknown