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J. Biol. Chem., Vol. 277, Issue 48, 46763-46768, November 29, 2002
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From the Departments of We present evidence that the signal recognition
particle (SRP) recognizes signal sequences via the NG domain on
the SRP54 protein subunit. Using a recently developed
cross-linking method (Fancy, D. A., and Kodadek, T. (1999)
Proc. Natl. Acad. Sci. U. S. A. 96, 6020-6024;
Correction (1999) Proc. Natl. Acad. Sci. U. S. A.
96, 1317), we find that signal peptides cross-link to the
Escherichia coli SRP protein Ffh (the homologue of the
mammalian SRP54 subunit) via the NG domain. Within the NG domain, the
cross-linking site maps to the ras-like C-terminal subdomain termed the
G domain. This result stands in contrast to previous studies, which
concluded based on nascent chain cross-linking that the signal sequence bound to the adjacent M domain. As independent evidence of a direct binding interaction between the NG domain and the signal sequence, we
find that the NG domain of Ffh binds signal peptides as an isolated
entity. Our results suggest that the NG domain forms a substantial part
of the binding site for the signal sequence.
Mapping the Signal Sequence-binding Site on SRP Reveals
a Significant Role for the NG Domain*
§¶ and
**
Chemistry and
Biochemistry and Molecular Biology, University of
Massachusetts, Amherst, Massachusetts 01003
*
This work was supported in part by a grant from the National
Institutes of Health (GM34962 to L. M. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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