ffh Antibody

1. Here, theauthors show that the C-terminal helix of the signal-sequence-binding domain of signal recognition particle penetrates into the ribosomal tunnel and contacts the intra-tunnel loop of ribosomal protein uL23. PMID: 28134917
2. The kinetic analysis indicate that, at cellular concentrations of ribosomes and signal recognition particle (SRP), signal-anchor sequence (SAS) rapidly binds to translating ribosomes prior to the emergence of an SAS and forms an initial complex that rapidly rearranges to a more stable engaged complex. PMID: 29149347
3. Data indicate that the sigma factor 32 (sigma32)-Ffh (the protein subunit of signal recognition particle (SRP) interaction was significantly affected by mutations in this region that compromise the feedback regulation. PMID: 27052372
4. The cryo-electron microscopy structure of this 'false' early complex with EspP revealed an ordered M domain of SRP protein Ffh making two ribosomal contacts, and the NG domains of Ffh and FtsY forming a distorted, flexible heterodimer. PMID: 23563142
5. Data indicate that Escherichia coli Ffh protein bound to the large subunit of mitochondrial ribosomes, and could relieve, to some degree, the defect of Saccharomyces cerevisiae Oxa1 mutants. PMID: 23198851
6. Overexpression the M domain of Ffh inhibits the expression of membrane proteins. PMID: 20714446
7. crystal structure of the SRP:SR complex at 3.9 angstrom resolution and biochemical data revealing that the activated SRP:SR GTPase complex binds the distal end of the SRP hairpin RNA where GTP hydrolysis is stimulated PMID: 21330537
8. Results suggest that indeed, while FtsY-depletion affects earlier steps in the pathway (possibly translation), Ffh-depletion disrupts membrane protein biogenesis later during the targeting pathway by preventing their functional assembly in the membrane. PMID: 20161748
9. MsrA and MsrB are required to repair Ffh oxidized by reactive oxygen species produced by aerobic metabolism, establishing an as-yet undescribed link between protein targeting and oxidation PMID: 15057280
10. Ffh and FtsY form a complex in which both proteins reciprocally activate the GTPase reaction of one another PMID: 15383838
11. In free Ffh, the binding sites for 4.5S RNA and FtsY are occluded by strong domain-domain interactions. PMID: 15923378
12. FRET analysis of conformation of signal recognition particle protein Ffh from Escherichia coli PMID: 16005894
13. The signal recognition particle (SRP) RNA may coordinate the interaction of the SRP and the SRP receptor with ribosome recruitment and transfer to the translocon, explaining why the SRP RNA is an indispensable component of the protein targeting machinery. PMID: 17507650
14. the SRP and SR GTPases, without recruiting external regulatory factors, constitute a self-sufficient system that provides exquisite spatial and temporal control of a complex cellular process PMID: 19174514

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KEGG: ecj:JW5414

STRING: 316385.ECDH10B_2777