Structure and function of the molecular chaperone trigger factor
Newly synthesized proteins often require the assistance of molecular chaperones to efficiently fold into functional three-dimensional structures. At first, ribosome-associated chaperones guide the initial folding steps and protect growing polypeptide chains from misfolding and aggregation. After tha...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
[June 2010]
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| In: |
Biochimica et biophysica acta. Molecular cell research
Year: 2010, Volume: 1803, Issue: 6, Pages: 650-661 |
| ISSN: | 1879-2596 |
| DOI: | 10.1016/j.bbamcr.2010.01.017 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.bbamcr.2010.01.017 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0167488910000303 
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| Author Notes: | Anja Hoffmann, Bernd Bukau, Günter Kramer (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz) |
| Summary: | Newly synthesized proteins often require the assistance of molecular chaperones to efficiently fold into functional three-dimensional structures. At first, ribosome-associated chaperones guide the initial folding steps and protect growing polypeptide chains from misfolding and aggregation. After that folding into the native structure may occur spontaneously or require support by additional chaperones which do not bind to the ribosome such as DnaK and GroEL. Here we review the current knowledge on the best-characterized ribosome-associated chaperone at present, the Escherichia coli Trigger Factor. We describe recent progress on structural and dynamic aspects of Trigger Factor's interactions with the ribosome and substrates and discuss how these interactions affect co-translational protein folding. In addition, we discuss the newly proposed ribosome-independent function of Trigger Factor as assembly factor of multi-subunit protein complexes. Finally, we cover the functional cooperation between Trigger Factor, DnaK and GroEL in folding of cytosolic proteins and the interplay between Trigger Factor and other ribosome-associated factors acting in enzymatic processing and translocation of nascent polypeptide chains. |
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| Item Description: | Gesehen am 06.03.2023 |
| Physical Description: | Online Resource |
| ISSN: | 1879-2596 |
| DOI: | 10.1016/j.bbamcr.2010.01.017 |