Structure and function of the molecular chaperone trigger factor

• Verfasst von: Hoffmann, Anja [VerfasserIn]
• Verfasst von: Bukau, Bernd [VerfasserIn]
• Verfasst von: Kramer, Günter [VerfasserIn]
• Titel: Structure and function of the molecular chaperone trigger factor
• Verf.angabe: Anja Hoffmann, Bernd Bukau, Günter Kramer (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)
• E-Jahr: 2010
• Jahr: [June 2010]
• Umfang: 12 S.
• Fussnoten: Gesehen am 06.03.2023
• Titel Quelle: Enthalten in: Biochimica et biophysica acta / Molecular cell research
• Ort Quelle: Amsterdam [u.a.] : Elsevier, 1982
• Jahr Quelle: 2010
• Band/Heft Quelle: 1803(2010), 6 vom: Juni, Seite 650-661
• ISSN Quelle: 1879-2596
• DOI: doi:10.1016/j.bbamcr.2010.01.017
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Chaperone
• Sach-SW: Nascent chain
• Sach-SW: Protein folding
• Sach-SW: Ribosome
• Sach-SW: Trigger Factor
• K10plus-PPN: 1838267417

Abstract

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.