Nascent-chain biology



Below are our recent efforts on the nascent-chain biology.


【Nascent chain folding and the chaperone effects】 To understand the translation-coupled protein folding, we use a reconstituted cell-free translation system of E. coli (PURE system) and chaperones such as GroEL and DnaK (Hsp70 in E. coli).



【Selected publications】

-Niwa T, Uemura E, Matsuno Y, *Taguchi, H.
Translation-coupled protein folding assay using a protease to monitor the folding status. 
Protein Science 28, 1252-1261 (2019) [Protein Science Best Paper award 2019]

-Uemura E, Niwa T, Minami S, Takemoto K, Fukuchi S, Machida K, Imataka H, Ueda T, Ota M, *Taguchi H.
Large-scale aggregation analysis of eukaryotic proteins reveals an involvement of intrinsically disordered regions in protein folding.
Sci Rep 8:678. (2018))

-Niwa, T, Kanamori T, *Ueda, T, *Taguchi H.
Global analysis of chaperone effects using a reconstituted cell-free translation system
Proc Natl Acad Sci USA 109, 8937-8942 (2012)

-Niwa, T., Ying, B.-W., Saito, K., Jin, W. Z., Takada, S., Ueda, T. *Taguchi, H.
Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins.
Proc Natl Acad Sci USA 106, 4201-4206 (2009)


【Noncanonical translation dynamics】We conducted a large-scale analysis of translatioal pausing. The study on the pausing led to the discovery of a novel noncanonical translation dynamics (Intrinsic ribosome destabilization: IRD), and we are currently working to explore the frontier of the protein world.



【Selected publications】
-Chadani Y, Niwa T, Izumi T, Sugata N, Nagao A, Suzuki T, Chiba S, *Ito K, *Taguchi H.
Intrinsic ribosome destabilization underlies translation and provides an organism with a strategy of environmental sensing.
Mol Cell 68, 528-539 (2017)

-Chadani Y, Niwa T, Chiba S, *Taguchi H, *Ito K.
Integrated in vivo and in vitro nascent chain profiling reveals widespread translational pausing.
Proc Natl Acad Sci USA 113, E829-38 (2016)