Substrate twinning activates the signal recognition particle and its receptor

Nature

Volumn 427, Issue 6971, 2004, Pages 215-221

  Egea, Pascal F ^a   Shan, Shu Ou ^a,b   Napetschnig, Johanna ^a   Savage, David F ^a   Walter, Peter ^a,b   Stroud, Robert M ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CELL MEMBRANES; DIMERS; DISSOCIATION; HYDROLYSIS;

RIBOSOMES; SIGNAL RECEPTION PARTICLES (SRP); SIGNAL SEQUENCES;

ENZYMES;

DOCKING PROTEIN; GUANOSINE TRIPHOSPHATASE; SIGNAL RECOGNITION PARTICLE;

SIGNAL;

ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HYDROLYSIS; PRIORITY JOURNAL; RIBOSOME; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; BIOLOGICAL TRANSPORT; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME ACTIVATION; GTP PHOSPHOHYDROLASES; GUANOSINE TRIPHOSPHATE; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SORTING SIGNALS; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECEPTORS, PEPTIDE; RIBOSOMES; SEQUENCE ALIGNMENT; SIGNAL RECOGNITION PARTICLE; SUBSTRATE SPECIFICITY; THERMUS;

EID: 0347584006     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02250     Document Type: Article

References (38)

1. Keenan, R. J., Freymanm, D. M., Stroud, R. M. & Walter, P. The signal recognition particle. Annu. Rev. Biochem. 70, 755-775 (2001).
2. Stroud, R. M. & Walter, P. Signal sequence recognition and protein targeting. Curr. Opin. Struct. Biol. 9, 754-759 (1999).
3. Pool, M. R., Stumm, J., Fulga, T. A., Sinning, I. & Dobberstein, B. Distinct modes of signal recognition particle interaction with the ribosome. Science 297, 1345-1348 (2002).
4. Rinke-Appel, J. et al. Crosslinking of 4.5S RNA to the Escherichia coli ribosome in the presence or absence of the protein Ffh. RNA 8, 612-625 (2002).
5. Gilmore, R., Blobel, G. & Walter, P. Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle. J. Cell Biol. 95, 463-469 (1982).
6. Meyer, D. I., Krause E. & Dobberstein, B. Secretory protein translocation across membranes - the role of the 'docking protein'. Nature 297, 647-650 (1982).
7. Walter, P. & Blobel, G. Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc. Natl Acad. Sci. USA 77, 7112-7116 (1980).
8. Gilmore R., Walter, P. & Blobel, G. Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor. J. Cell Biol. 95, 470-477 (1982).
9. Bekmann, R. et al. Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex. Science 278, 2123-2126 (1997).
10. Menetret, J. F. et al. The structure of ribosome-channel complexes engaged in protein translocation. Mol. Cell 6, 1219-1232 (2000).
11. Beckmann, R. et al. Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell 107, 361-372 (2001).
12. Miller, J. D., Wilhelm, H., Gierasch, L., Gilmore, R. & Walter, P. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Nature 366, 351-354 (1993).
13. Miller, J. D., Bernstein, H. D. & Walter, P. Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor. Nature 367, 657-659 (1994).
14. Powers, T. & Walter, P. Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases. Science 269, 1422-1424 (1995).
15. Keenan, R. J., Freymann, D. M., Walter, P. & Stroud, R. M. Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell 94, 181-191 (1998).
16. Montoya, G., Svensson, C., Luirink, J. & Sinning, I. Crystal structure of the NG domain from the signal-recognition particle receptor FisY. Nature 385, 365-368 (1997).
17. Freymann, D. M., Keenan, R. J., Stroud, R. M. & Walter, P. Structure of the conserved GTPase domain of the signal recognition particle. Nature 385, 361-364 (1997).
18. Ramirez, U. D. et al. Structural basis for mobility in the 1.1 Å crystal structure of the NG domain of Thermes aquaticus Ffh. J. Mol. Biol. 320, 783-799 (2002).
19. Vetter, I. R. & Wittinghofer, A. The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304 (2001).
20. Montoya, G., Kaat, K., Moll, R., Schafer, G. & Sinning, I. The crystal structure of the conserved GTPase of SRP54 from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for the SRP-SRP receptor complex. Struct. Fold. Des. 8, 515-525 (2000).
21. Rapiejko, P. J. & Gilmore, R. Empty site forms of the SRP54 and SR α GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum. Cell 89, 703-713 (1997).
22. Peluso, P., Shan, S. O., Nock, S., Ilerschlag, D., Walter P. Role of SRP RNA in the GTPase cycles of Ffh and FtsY. Biochemistry 40, 15224-15233 (2001).
23. Shan, S. & Walter, P. Induced nucleotide specificity in a GTPase. Proc. Natl Acad. Sci. USA 100, 4480-4485 (2003).
24. Padmanabhan, S. & Freymann, D. M. The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPase. Structure 9, 859-867 (2001).
25. Smith, P. C. et al. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149 (2002).
26. Schindelin, H., Kisker, C., Schlessman, I. L., Howard, I. B. & Rees, D. C. Structure of ADP × AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature 387, 370-376 (1997).
27. Seewald, M. J., Korner, C., Wittinghofer, A. & Vetter, I. R. RanGAP mediates GTP hydrolysis without an arginine finger. Nature 415, 662-666 (2002).
28. Tesmer, I. J., Berman, D. M., Gilman, A. G. & Sprang, S. R. Structure of RGS4 bound to AIF4-activated Gi α: Stabilization of the transition state for GTP hydrolysis. Cell 89, 251-261 (1997).
29. Srinivassa, S. D., Watson, N., Overton, M. C. & Blumer, K. I. Mechanism of RGS4, a GTPase-activating protein for G-protein α subunits. J. Biol. Chem. 273, 1529-1533 (1998).
30. Slep, K. C. et al. Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å. Nature 409, 1071-1077 (2001).
31. Focia, P. J., Shepotinovskaya, I. V., Seidler, I. A. & Freymann, D. M. Heterodimeric GTPase core of the 5RP targeting complex. Science (in the press).
32. Otwinowski, Z. & Minor, W. Processing X-ray data in oscillation mode. Methods Enzymol. 276, 307-326 (1996).
33. Navaza, J. Implementation of molecular replacement in AMoRe. Acta Crystallogr. D 57, 1367-1372 (2001).
34. Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
35. Muller, K. et al. Moloc. Bull. Soc. Chim. Belg. 97, 655-667 (1988).
36. Shepotinovskaya, I. V. & Freymann, D. M. Conformational change of the N-domain on formation of the complex between the GTPase domains of Thermus aquaticus and FtsY. Biochim. Biophys. Acta 1597, 107-114 (2002).
37. DeLano, W. L. The PyMOL Molecular Graphics System 〈 http://www.pymol.org/〉 2003).
38. Philipssen, A. DINO: Visualizing Structural Biology 〈 http://www.dino3d.org〉 (2002).