Archeal

A functional archeal SRP is organized around two proteins, SRP19 and SRP54 that assemble on SRP RNA. ❋ Pascal F. Egea Et Al. (2008)

Pfu - SRP54 and SRP19 (in press in PloS One) have been incorporated into a model of the archeal SRP•SR targeting complex. ❋ Pascal F. Egea Et Al. (2008)

We have built a model of the core of the archeal targeting complex based on structures of the ❋ Pascal F. Egea Et Al. (2008)

Sequence analysis suggests that these features are conserved throughout all archeal receptors ❋ Pascal F. Egea Et Al. (2008)

These properties appear to be conserved in all archeal receptor sequences. ❋ Pascal F. Egea Et Al. (2008)

While FtsY and some other bacterial receptors possess an extra N-terminal A domain of variable size and sequence, most bacterial and archeal receptors are further streamlined and reduced to the strictly conserved NG core. ❋ Pascal F. Egea Et Al. (2008)

The sequence of Pfu-FtsY is aligned against 12 FtsY sequences from archeons representative of all families constituting the archeal kingdom. ❋ Pascal F. Egea Et Al. (2008)

While the overall architecture of the archeal receptor resembles its previously described bacterial homologues from the SRP / SR GTPases family, the structure of ❋ Pascal F. Egea Et Al. (2008)

A model for the interaction between SRP and SR in the archeal and eukaryotic core of the targeting complex The targeting complex is formed when SRP interacts with its receptor ( ❋ Pascal F. Egea Et Al. (2008)

Figure 4B), helix αN1 of the non-archeal homologues is bent, resulting in an N terminal extension that packs against the surface of the N / G domain including C terminal helix α7 ( ❋ Pascal F. Egea Et Al. (2008)