A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor.

@article{Weiche2008ACN,
  title={A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor.},
  author={Benjamin Weiche and Jonas Buerk and Sandra Angelini and Emile Schiltz and J{\"o}rg Oliver Thumfart and Hans-Georg Koch},
  journal={Journal of molecular biology},
  year={2008},
  volume={377 3},
  pages={761-73}
}
Different from eukaryotes, the bacterial signal recognition particle (SRP) receptor lacks a membrane-tethering SRP receptor (SR) beta subunit and is composed of only the SR alpha homologue FtsY. FtsY is a modular protein composed of three domains. The N- and G-domains of FtsY are highly similar to the corresponding domains of Ffh/SRP54 and SR alpha and constitute the essential core of FtsY. In contrast, the weakly conserved N-terminal A-domain does not seem to be essential, and its exact… CONTINUE READING
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