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

Kamran Rizzolo, Angela Yeou Hsiung Yu, 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 and Walid A. Houry ()
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Kamran Rizzolo: University of Toronto
Angela Yeou Hsiung Yu: University of Toronto
Adedeji Ologbenla: University of Toronto
Sa Rang Kim: University of Toronto
Haojie Zhu: Hokkaido University
Koichiro Ishimori: Hokkaido University
Guillaume Thibault: University of Toronto
Elisa Leung: University of Toronto
Yi Wen Zhang: University of Toronto
Mona Teng: University of Toronto
Marta Haniszewski: University of Toronto
Noha Miah: University of Toronto
Sadhna Phanse: University of Toronto
Zoran Minic: University of Regina
Sukyeong Lee: Baylor College of Medicine
Julio Diaz Caballero: University of Toronto
Mohan Babu: University of Regina
Francis T. F. Tsai: Baylor College of Medicine
Tomohide Saio: Tokushima University
Walid A. Houry: University of Toronto

Nature Communications, 2021, vol. 12, issue 1, 1-18

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

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-020-20553-x

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DOI: 10.1038/s41467-020-20553-x

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