Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex

• DOI: 10.1038/s41467-020-20553-x
• Publication Date: 2021-01-12T18:36:08Z
• Authors: Kamran Rizzolo; Angela Yeou Hsiun...; Adedeji Ologbenla; Sa Rang Kim; Haojie Zhu; Koichiro Ishimori; Guillaume Thibault; Elisa Leung; Yi Wen Zhang; Mona Teng; Marta Haniszewski; Noha Miah; Sadhna Phanse; Zoran Minic; Sukyeong Lee; Julio Diaz Caballero; Mohan Babu; Francis T. F. Tsai; Tomohide Saio; Walid A. Houry
• Keywords: Chaperone (clinical); Proteolysis; Protein Degradation; Cooperativity; rpoS

Abstract A functional association is uncovered between the ribosome-associated trigger factor (TF) chaperone and ClpXP degradation complex. Bioinformatic analyses demonstrate conservation of close proximity tig , gene coding for TF, genes ClpXP, suggesting a interaction. The effect TF on ClpXP-dependent varies based nature substrate. While some substrates are slowed down or unaffected by surprisingly, increases rate third class substrates. These include λ phage replication protein λO, master regulator stationary phase RpoS, SsrA-tagged proteins. Globally, acts to enhance about 2% newly synthesized found interact through multiple sites with ClpX in highly dynamic fashion promote degradation. This chaperone–protease cooperation constitutes unique likely ancestral aspect cellular homeostasis which as an adaptor ClpXP.