Trigger Factor-Induced Nascent Chain Dynamics Changes Suggest Two Different Chaperone-Nascent Chain Interactions during Translation

Koubek, Jiří; Chang, Yi-Che; Yang, S.Y. Cindy; Huang, Joseph Jen‐Tse

doi:10.1016/j.jmb.2017.03.029

Cited by 2 publications

(2 citation statements)

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“…As the nascent chain emerges from the ribosome, the spatial constraints of the tunnel are relieved while the limiting impact of the ribosome on the conformational space of the nascent chain partially remains. Supported by studies on multiple model proteins ( Hsu et al, 2007 ; Ellis et al, 2008 ; Ellis et al, 2009 ; Kelkar et al, 2012 ; Holtkamp et al, 2015 ; Kim et al, 2015 ; Koubek et al, 2017 ; Nilsson et al, 2017 ; Farias-Rico et al, 2018 ; Mercier and Rodnina, 2018 ; Kemp et al, 2019 ; Liutkute et al, 2020a ) it is estimated that at least 30% of the cytosolic E. coli proteome folds independently of chaperones ( Ciryam et al, 2013 ). Folding of these proteins is therefore solely determined by the intrinsic biophysical properties of the amino acid sequence and the influence of the ribosome.…”

Section: The Ribosome As the Platform For Protein Maturationmentioning

confidence: 99%

Mechanisms of Cotranslational Protein Maturation in Bacteria

Koubek

Schmitt

Galmozzi

2021

Front. Mol. Biosci.

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Growing cells invest a significant part of their biosynthetic capacity into the production of proteins. To become functional, newly-synthesized proteins must be N-terminally processed, folded and often translocated to other cellular compartments. A general strategy is to integrate these protein maturation processes with translation, by cotranslationally engaging processing enzymes, chaperones and targeting factors with the nascent polypeptide. Precise coordination of all factors involved is critical for the efficiency and accuracy of protein synthesis and cellular homeostasis. This review provides an overview of the current knowledge on cotranslational protein maturation, with a focus on the production of cytosolic proteins in bacteria. We describe the role of the ribosome and the chaperone network in protein folding and how the dynamic interplay of all cotranslationally acting factors guides the sequence of cotranslational events. Finally, we discuss recent data demonstrating the coupling of protein synthesis with the assembly of protein complexes and end with a brief discussion of outstanding questions and emerging concepts in the field of cotranslational protein maturation.

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Section: The Ribosome As the Platform For Protein Maturationmentioning

confidence: 99%

Mechanisms of Cotranslational Protein Maturation in Bacteria

Koubek

Schmitt

Galmozzi

2021

Front. Mol. Biosci.

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“…TF can be recruited to the proximity of polypeptide exit via docking onto the L23 protein of the large ribosome subunit (1)(2)(3)(4). The interaction of TF with nascent polypeptides and ribosomes is dynamic and is governed by properties of the nascent polypeptide chain emerging from the ribosome (5)(6)(7)(8)(9)(10). By acting on nascent polypeptides, TF can decrease the folding rate, change the folding mechanism, and consequently improve the efficiencies of polypeptide folding and even complex assembly (9,(11)(12)(13)(14).…”

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confidence: 99%

Exploring the roles of substrate‐binding surface of the chaperone site in the chaperone activity of trigger factor

et al. 2018

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Trigger factor (TF) is a key component of the prokaryotic chaperone network, which is involved in many basic cellular processes, such as protein folding, protein trafficking, and ribosome assembly. The major chaperone site of TF has a cradle-like structure in which protein substrate may fold without interference from other proteins. Here, we investigated in vivo and in vitro the roles of hydrophobic and charged patches on the edge and interior of cradle during TF-assisted protein folding. Our results showed that most of the surface of the cradle was involved in TF-assisted protein folding, which was larger than found in early studies. Although the inner surface of cradle was mostly hydrophobic, both hydrophobic and electrostatic patches were indispensable for TF to facilitate correct protein folding. However, hydrophobic patches were more important for the antiaggregation activity of TF. Furthermore, it was found that the patches on the surface of cradle were involved in TF-assisted protein folding in a spatial and temporal order. These results suggest that the folding-favorable interface between the cradle and substrate was dynamic during TF-assisted protein folding, which enabled TF to be involved in the folding of substrate in an aggressive manner rather than acting as a classic holdase.-Fan, D., Cao, S., Zhou, Q., Zhang, Y., Yue, L., Han, C., Yang, B., Wang, Y., Ma, Z., Zhu, L., Liu, C. Exploring the roles of substrate-binding surface of chaperone site in the chaperone activity of trigger factor.

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Trigger Factor-Induced Nascent Chain Dynamics Changes Suggest Two Different Chaperone-Nascent Chain Interactions during Translation

Cited by 2 publications

References 57 publications

Mechanisms of Cotranslational Protein Maturation in Bacteria

Mechanisms of Cotranslational Protein Maturation in Bacteria

Exploring the roles of substrate‐binding surface of the chaperone site in the chaperone activity of trigger factor

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