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• W2061388232 abstract "Trigger factor (TF) is the first chaperone to interact with nascent chains and facilitate their folding within bacteria. TF possesses a three-state equilibrium in vivo: monomeric TF bound to ribosome, free monomeric, and dimeric TF in cytoplasm. TF consists of an N-terminal ribosome binding domain, a middle peptidyl–prolyl cis/trans isomerase (PPIase) domain and a C-terminal domain involved in substrate binding and dimerization. Investigation of the effect of C-terminal 13 region on TF structure and function will help to further the understanding of its mechanism as a chaperone in vitro and in vivo. Here we present TF419, a TF mutant from which the C-terminal 13 residues were deleted to investigate the role of these residues in the structure stability and function of intact molecules. Small angle X-ray scattering (SAXS), fluorescence measurements and limited proteolysis results suggested that TF transitioned to a compact conformation when the Cterminal 13 residues were truncated. Further biochemical results reveal that TF dimerization was decreased as a result of the truncation. These results suggested that the C-terminal 13 residues play an important role in structural stability and chaperone function of TF." @default.
• W2061388232 created "2016-06-24" @default.
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• W2061388232 date "2014-02-01" @default.
• W2061388232 modified "2023-10-18" @default.
• W2061388232 title "C-terminal 13-residue Truncation Induces Compact Trigger Factor Conformation and Severely Impairs its Dimerization Ability" @default.
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• W2061388232 doi "https://doi.org/10.2174/092986652105140218114955" @default.
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