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ID 116608
Rizzolo, Kamran University of Toronto|Dewpoint Therapeutics
Yu, Angela Yeou Hsiung University of Toronto|Pfizer
Ologbenla, Adedeji University of Toronto
Kim, Sa Rang University of Toronto
Zhu, Haojie Hokkaido University
Ishimori, Koichiro Hokkaido University
Thibault, Guillaume University of Toronto|Nanyang Technological University
Leung, Elisa University of Toronto
Zhang, Yi Wen University of Toronto
Teng, Mona University of Toronto
Haniszewski, Marta University of Toronto
Miah, Noha University of Toronto
Phanse , Sadhna University of Toronto|University of Regina
Minic, Zoran University of Regina|University of Ottawa
Lee, Sukyeong Baylor College of Medicine
Caballero, Julio Diaz University of Toronto
Babu, Mohan University of Regina
Tsai, Francis T. F. Baylor College of Medicine
Houry, Walid A. University of Toronto
Content Type
Journal Article
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.
Journal Title
Nature Communications
Springer Nature
Start Page
Published Date
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Institute of Advanced Medical Sciences