Recombinant Escherichia coli Trigger factor (tig)

1. by combining the transcriptome and phenotype results, a physiological mechanism underlying the impact of TF deletion on the transcriptome profile was proposed. PMID: 27279076
2. The structures reveal distinct degrees of flexibility for the different trigger factor domains, a conformational rearrangement of the N-terminal ribosome-binding domain upon ribosome binding, and an increase in rigidity within trigger factor when the nascent peptide chain is extended. PMID: 27320387
3. Trigger factor prevents signal recognition particle binding to the majority of ribosomes, except those presenting SRP-specific signal sequences. PMID: 24939037
4. Fused the ANTXR2 ectodomain to the C-terminus of bacterial Trigger Factor (TF), and the fusion protein was overly expressed as a dominant soluble protein in E coli. PMID: 24380801
5. ribosome- and Trigger Factor-specific activities together constitute an efficient mechanism to prevent or even revert premature folding, effectively limiting misfolded intermediates during protein synthesis PMID: 22921937
6. Studies of the Escherichia coli chaperone trigger factor (TF) reveal that, though TF can interact with many polypeptides, beta-barrel outer-membrane proteins are the most prominent substrates PMID: 22153074
7. mutant TF lacking the PPIase domain is more efficient than wild-type TF in enhancing the folding yield of multi-domain proteins such as firefly luciferase PMID: 20659464
8. contact with trigger factor with Tat protein was strictly dependent on the context of the translating ribosome, started early in biogenesis when the nascent chain left the ribosome near L23, and persisted until the chain reached its full length PMID: 15606765
9. structural integrity of the C-terminus contributes to both the chaperone function of TF and the stability of the dimeric form PMID: 16380200
10. Supports productive de novo folding by shielding nascent polypeptides on the ribosome thereby preventing untimely degradation or aggregation processes. PMID: 16407311
11. the molecular environment of a signal sequence at the ribosome depends on downstream sequence elements that can cause an alternate recruitment of signal recognition particle and the ribosome-associated chaperone Trigger factor to a growing nascent chain PMID: 16421097
12. the SRP appears perfectly capable of distinguishing SA sequences from signal sequences in secretory proteins at an early stage in biogenesis PMID: 16551615
13. Escherichia coli trigger factor C-terminal domain represents the central module of its chaperone activity PMID: 16926148
14. there are two regions on TF along which nascent chains can interact, the NC-domains as the main site and the PPIase domain as an auxiliary site PMID: 17296610
15. Sequence of molecular interactions of Escherichia coli TF and nascent chains during translation was identified. PMID: 18497744
16. Trigger factor (TF) might be important in responding to stress damage, such as heat shock. PMID: 18539163
17. Ribosome-free TF stably associates with and rescues from misfolding a large repertoire of full-length proteins; study identifies over 170 members of this cytosolic Escherichia coli TF substrate proteome, including ribosomal protein S7. PMID: 19737520

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KEGG: ecj:JW0426

STRING: 316385.ECDH10B_0392