Abstract
The signal-recognition particle (SRP) and its receptor (SR) function in the co-translational targeting of nascent protein–ribosome complexes to the membrane translocation apparatus1. The SRP protein subunit (termed Ffh in bacteria) that recognizes the signal sequence of nascent polypeptides is a GTPase, as is the SR-α subunit (termed FtsY)2,3. Ffh and FtsY interact directly, each stimulating the GTP hydrolysis activity of the other4. The sequence of Ffh suggests three domains: an amino-terminal N domain of unknown function, a central GTPase G domain, and a methionine-rich M domain that binds both SRP RNA and signal peptides5,6. Sequence conservation suggests that structurally similar N and G domains are present in FtsY7,8. Here we report the structure of the nucleotide-free form of the NG fragment of Ffh. Consistent with a role for apo Ffh in protein targeting, the side chains of the empty active-site pocket form a tight network of interactions which may stabilize the nucleotide-free protein. The structural relationship between the two domains suggests that the N domain senses or controls the nucleotide occupancy of the GTPase domain. A structural subdomain unique to these evolutionarily conserved GTPases constitutes them as a distinct subfamily in the GTPase superfamily9.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Rent or buy this article
Prices vary by article type
from$1.95
to$39.95
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Walter, P. & Johnson, A. E. Annu. Rev. Cell Biol. 10, 87–119 (1994).
Miller, J. D., Bernstein, H. D. & Walter, P. Nature 367, 657–659 (1994).
Kusters, R. et al. FEBS Lett. 372, 253–258 (1995).
Powers, T. & Walter, P. Science 269, 1422–1424 (1995).
Zopf, D., Bernstein, H. D. & Walter, P. J. Cell Biol. 120, 1113–1121 (1993).
Römisch, K., Webb, J., Lingelbach, K., Gausepohl, H. & Dobberstein, B. J. Cell Biol. 111, 1793–1802 (1990).
Bernstein, H. D. et al. Nature 340, 482–486 (1989).
Römisch, K. et al. Nature 340, 478–482 (1989).
Bourne, H. R., Sanders, D. A. & McCormick, F. Nature 348, 125–132 (1990).
Pai, E. F. et al. Nature 341, 209–214 (1989).
Czworkowski, J., Wang, J., Steitz, T. A. & Moore, P. B. EMBO J. 13, 3661–3668 (1994).
Ævarsson, A. et al. EMBO J. 13, 3669–3677 (1994).
Noel, J. P., Hamm, H. E. & Sigler, P. B. Nature 366, 654–663 (1993).
Lütcke, H., High, S., Römisch, K., Ashford, A. J. & Dobberstein, B. EMBO J. 11, 1543–1551 (1992).
Bourne, H. R., Sanders, D. A. & McCormick, F. Nature 349, 117–127 (1991).
Sondek, J., Lambright, D. G., Noel, J. P., Hamm, H. E. & Sigler, P. B. Nature 372, 276–279 (1994).
Berchtold, H. et al. Nature 365, 126–132 (1993).
Prive, G. G. et al. Proc. Natl Acad. Sci. USA 89, 3649–3653 (1992).
Al-Karadaghi, S., Ævarsson, A., Garber, M., Zheltonosova, J. & Liljas, A. Structure 4, 555–565 (1996).
Miller, J. D., Wilhelm, H., Gierasch, L., Gilmore, R. & Walter, P. Nature 366, 351–354 (1993).
Milburn, M. V. et al. Science 247, 939–945 (1990).
Lambright, D. G. et al. Nature 379, 311–319 (1996).
Otwinowski, Z. in Data Collection and Processing (eds Sawyer, L., Isaacs, N. W. & Bailey, S.) 55–62 (SERC Daresbury Laboratory, Warrington, 1993).
Collaborative Computational Project Number 4. Acta Crystallogr. D 50, 760–763 (1994).
Read, R. J. Acta Crystallogr. A 42, 140–149 (1986).
Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Acta Crystallogr. A 47, 110–119 (1991).
Brünger, A. T. X-PLOR: A System for X-Ray Crystallography and NMR (Yale Univ. Press, New Haven, 1992).
Kjeldgaard, M., Nissen, P., Thirup, S. & Nyborg, J. Structure 1, 35–50 (1993).
Amor, J. C., Harrison, D. H., Kahn, R. A. & Ringe, D. Nature 372, 704–708 (1994).
Evans, S. V. J. Mol. Graph. 11, 134–138 (1993).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Freymann, D., Keenan, R., Stroud, R. et al. Structure of the conserved GTPase domain of the signal recognition particle. Nature 385, 361–364 (1997). https://doi.org/10.1038/385361a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/385361a0
This article is cited by
-
Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp
Nature Communications (2022)
-
SRP54 Negatively Regulates IFN-Beta Production and Antiviral Response by Targeting RIG-I and MDA5
Virologica Sinica (2021)
-
Protein Transport Across the Bacterial Plasma Membrane by the Sec Pathway
The Protein Journal (2019)
-
The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective
Current Microbiology (2017)
-
Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon
Nature Communications (2016)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.