PMID:15923378
| Citation |
Buskiewicz, I, Kubarenko, A, Peske, F, Rodnina, MV and Wintermeyer, W (2005) Domain rearrangement of SRP protein Ffh upon binding 4.5S RNA and the SRP receptor FtsY. RNA 11:947-57 |
|---|---|
| Abstract |
The signal recognition particle (SRP) mediates membrane targeting of translating ribosomes displaying a signal-anchor sequence. In Escherichia coli, SRP consists of 4.5S RNA and a protein, Ffh, that recognizes the signal peptide emerging from the ribosome and the SRP receptor at the membrane, FtsY. In the present work, we studied the interactions between the NG and M domains in Ffh and their rearrangements upon complex formation with 4.5S RNA and/or FtsY. In free Ffh, the NG and M domains are facing one another in an orientation that allows cross-linking between positions 231 in the G domain and 377 in the M domain. There are binding interactions between the two domains, as the isolated domains form a strong complex. The interdomain contacts are disrupted upon binding of Ffh to 4.5S RNA, consuming a part of the total binding energy of 4.5S RNA-Ffh association that is roughly equivalent to the free energy of domain binding to each other. In the SRP particle, the NG domain binds to 4.5S RNA in a region adjacent to the binding site of the M domain. Ffh binding to FtsY also requires a reorientation of NG and M domains. These results suggest that in free Ffh, the binding sites for 4.5S RNA and FtsY are occluded by strong domain-domain interactions which must be disrupted for the formation of SRP or the Ffh-FtsY complex. |
| Links |
PubMed PMC1370779 Online version:10.1261/rna.7242305 |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Sequence; Binding Sites; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Fluorescence Resonance Energy Transfer; Molecular Sequence Data; Protein Structure, Tertiary; RNA, Bacterial; RNA, Ribosomal/chemistry; RNA, Ribosomal/metabolism; Receptors, Cytoplasmic and Nuclear/chemistry; Receptors, Cytoplasmic and Nuclear/metabolism; Signal Recognition Particle/chemistry; Signal Recognition Particle/genetics; Signal Recognition Particle/metabolism |
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