Member database | PANTHER |
PANTHER type | family |
Description Imported from IPR005215
The trigger factor is found in several prokaryotes, and is involved in protein export. Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. It acts as a chaperone by maintaining the newly synthesised protein in an open conformation. It consists of three domains, an N-terminal ribosome-binding domain (RBD), a central peptidyl-prolyl cis/trans isomerase (PPIase) domain and a C-terminal substrate-binding domain (SBD) which is stabilised by a linker between the RBD and PPIase domains
[1, 2, 3]. The association between its N-terminal domain with the ribosomal protein L23 located next to the peptide tunnel exit is essential for the interaction with nascent polypeptides and its in vivo function. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY)
[1].
The trigger factor-like protein included in this entry can be found in plant chloroplasts, where it may be involved in protein export.
References Imported from IPR005215
1.Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains. Kramer G, Rutkowska A, Wegrzyn RD, Patzelt H, Kurz TA, Merz F, Rauch T, Vorderwulbecke S, Deuerling E, Bukau B. J. Bacteriol. 186, 3777-84, (2004). View articlePMID: 15175291
2.Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Ferbitz L, Maier T, Patzelt H, Bukau B, Deuerling E, Ban N. Nature 431, 590-6, (2004). View articlePMID: 15334087