SIMIBI twins in protein targeting and localization

Nature Structural and Molecular Biology

Volumn 20, Issue 7, 2013, Pages 776-780

  Bange, Gert ^a,b   Sinning, Irmgard ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; NUCLEOTIDE BINDING PROTEIN; PROTEIN SIMIBI; SIGNAL RECOGNITION PARTICLE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

BACILLUS SUBTILIS; BACTERIAL GENOME; BINDING SITE; CELL DIVISION; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ENDOPLASMIC RETICULUM; FLAGELLUM; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; PROTEIN TARGETING; REVIEW; VIBRIO CHOLERAE;

ADENOSINE TRIPHOSPHATASES; BACTERIA; CARRIER PROTEINS; GTP PHOSPHOHYDROLASES; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION; PROTEIN TRANSPORT;

EID: 84880165593     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2605     Document Type: Review

References (57)

1. Leipe, D.D., Wolf, Y.I., Koonin, E.V. & Aravind, L. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol. 317, 41-72 (2002).
2. Kimple, A.J., Bosch, D.E., Giguere, P.M. & Siderovski, D.P. Regulators of G-protein signaling and their G substrates: promises and challenges in their use as drug discovery targets. Pharmacol. Rev. 63, 728-749 (2011).
3. Wittinghofer, A. & Vetter, I.R. Structure-function relationships of the G domain, a canonical switch motif. Annu. Rev. Biochem. 80, 943-971 (2011).
4. Bourne, H.R., Sanders, D.A. & McCormick, F. The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348, 125-132 (1990).
5. Gasper, R., Meyer, S., Gotthardt, K., Sirajuddin, M. & Wittinghofer, A. It takes two to tango: regulation of G proteins by dimerization. Nat. Rev. Mol. Cell Biol. 10, 423-429 (2009).
6. Saraste, M., Sibbald, P.R. & Wittinghofer, A. The P-loop-a common motif in ATP-and GTP-binding proteins. Trends Biochem. Sci. 15, 430-434 (1990).
7. Vetter, I.R. & Wittinghofer, A. The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304 (2001).
8. Akopian, D., Shen, K., Zhang, X. & Shan, S.O. Signal recognition particle: an essential protein-targeting machine. Annu. Rev. Biochem. published online, http://dx.doi.org/10.1146/annurev-biochem-072711-164732 (13 February 2013).
9. Grudnik, P., Bange, G. & Sinning, I. Protein targeting by the signal recognition particle. Biol. Chem. 390, 775-782 (2009).
10. 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).
11. Montoya, G., Svensson, C., Luirink, J. & Sinning, I. Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature 385, 365-368 (1997).
12. Egea, P.F. et al. Substrate twinning activates the signal recognition particle and its receptor. Nature 427, 215-221 (2004).
13. Focia, P.J., Shepotinovskaya, I.V., Seidler, J.A. & Freymann, D.M. Heterodimeric GTPase core of the SRP targeting complex. Science 303, 373-377 (2004).
14. Estrozi, L.F., Boehringer, D., Shan, S.O., Ban, N. & Schaffitzel, C. Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor. Nat. Struct. Mol. Biol. 18, 88-90 (2011).
15. Siu, F.Y., Spanggord, R.J. & Doudna, J.A. SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting. RNA 13, 240-250 (2007).
16. Ataide, S.F. et al. The crystal structure of the signal recognition particle in complex with its receptor. Science 331, 881-886 (2011).
17. Shen, K., Arslan, S., Akopian, D., Ha, T. & Shan, S.O. Activated GTPase movement on an RNA scaffold drives co-translational protein targeting. Nature 492, 271-275 (2012).
18. Zhang, X. et al. Direct visualization reveals dynamics of a transient intermediate during protein assembly. Proc. Natl. Acad. Sci. USA 108, 6450-6455 (2011).
19. Holtkamp, W. et al. Dynamic switch of the signal recognition particle from scanning to targeting. Nat. Struct. Mol. Biol. 19, 1332-1337 (2012).
20. Parlitz, R. et al. Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix. J. Biol. Chem. 282, 32176-32184 (2007).
21. Stjepanovic, G. et al. Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting. J. Biol. Chem. 286, 23489-23497 (2011).
22. de Leeuw, E. et al. Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity. EMBO J. 19, 531-541 (2000).
23. Bacher, G., Lutcke, H., Jungnickel, B., Rapoport, T.A. & Dobberstein, B. Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting. Nature 381, 248-251 (1996).
24. Bange, G. et al. Structural basis for the molecular evolution of SRP-GTPase activation by protein. Nat. Struct. Mol. Biol. 18, 1376-1380 (2011).
25. Hegde, R.S. & Keenan, R.J. Tail-anchored membrane protein insertion into the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 12, 787-798 (2011).
26. Formighieri, C., Cazzaniga, S., Kuras, R. & Bassi, R. Biogenesis of photosynthetic complexes in the chloroplast of Chlamydomonas reinhardtii requires ARSA1, a homolog of prokaryotic arsenite transporter and eukaryotic TRC40 for guided entry of tail-anchored proteins. Plant J. 73, 850-861 (2013).
27. Suloway, C.J., Chartron, J.W., Zaslaver, M. & Clemons, W.M. Jr. Model for eukaryotic tail-anchored protein binding based on the structure of Get3. Proc. Natl. Acad. Sci. USA 106, 14849-14854 (2009).
28. Denic, V., Doetsch, V. & Sinning, I. Endoplasmic reticulum targeting and insertion of tail-anchored membrane proteins by the GET pathway. Cold Spring Harb. Perspect. Biol. doi:10.1101/cshperspect.a013334 (in the press).
29. Bozkurt, G. et al. Structural insights into tail-anchored protein binding and membrane insertion by Get3. Proc. Natl. Acad. Sci. USA 106, 21131-21136 (2009).
30. Mateja, A. et al. The structural basis of tail-anchored membrane protein recognition by Get3. Nature 461, 361-366 (2009).
31. Chartron, J.W., Clemons, W.M. Jr. & Suloway, C.J. The complex process of GETting tail-anchored membrane proteins to the ER. Curr. Opin. Struct. Biol. 22, 217-224 (2012).
32. Sinning, I., Bange, G. & Wild, K. It takes two to Get3. Structure 19, 1353-1355 (2011).
33. Wang, F., Whynot, A., Tung, M. & Denic, V. The mechanism of tail-anchored protein insertion into the ER membrane. Mol. Cell 43, 738-750 (2011).
34. Mariappan, M. et al. The mechanism of membrane-associated steps in tail-anchored protein insertion. Nature 477, 61-66 (2011).
35. Stefer, S. et al. Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex. Science 333, 758-762 (2011).
36. Kubota, K., Yamagata, A., Sato, Y., Goto-Ito, S. & Fukai, S. Get1 stabilizes an open dimer conformation of Get3 ATPase by binding two distinct interfaces. J. Mol. Biol. 422, 366-375 (2012).
37. Lutkenhaus, J. Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring. Annu. Rev. Biochem. 76, 539-562 (2007).
38. Wu, W., Park, K.T., Holyoak, T. & Lutkenhaus, J. Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC. Mol. Microbiol. 79, 1515-1528 (2011).
39. Szeto, T.H., Rowland, S.L., Rothfield, L.I. & King, G.F. Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts. Proc. Natl. Acad. Sci. USA 99, 15693-15698 (2002).
40. Zhou, H. et al. Analysis of MinD mutations reveals residues required for MinE stimulation of the MinD ATPase and residues required for MinC interaction. J. Bacteriol. 187 629-638 (2005).
41. Lackner, L.L., Raskin, D.M. & de Boer, P.A. ATP-dependent interactions between Escherichia coli Min proteins and the phospholipid membrane in vitro. J. Bacteriol. 185, 735-749 (2003).
42. Cordell, S.C., Anderson, R.E. & Lowe, J. Crystal structure of the bacterial cell division inhibitor MinC. EMBO J. 20, 2454-2461 (2001).
43. Shen, B. & Lutkenhaus, J. Examination of the interaction between FtsZ and MinCN in E. coli suggests how MinC disrupts Z rings. Mol. Microbiol. 75, 1285-1298 (2010).
44. Hu, Z. & Lutkenhaus, J. Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ. J. Bacteriol. 182, 3965-3971 (2000).
45. Park, K.T., Wu, W., Lovell, S. & Lutkenhaus, J. Mechanism of the asymmetric activation of the MinD ATPase by MinE. Mol. Microbiol. 85, 271-281 (2012).
46. Park, K.T. et al. The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis. Cell 146, 396-407 (2011).
47. Scheffzek, K. et al. The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277, 333-338 (1997).
48. Chevance, F.F. & Hughes, K.T. Coordinating assembly of a bacterial macromolecular machine. Nat. Rev. Microbiol. 6, 455-465 (2008).
49. Bulyha, I., Hot, E., Huntley, S. & Sogaard-Andersen, L. GTPases in bacterial cell polarity and signalling. Curr. Opin. Microbiol. 14, 726-733 (2011).
50. Green, J.C. et al. Recruitment of the earliest component of the bacterial flagellum to the old cell division pole by a membrane-associated signal recognition particle family GTP-binding protein. J. Mol. Biol. 391, 679-690 (2009).
51. Guttenplan, S.B., Shaw, S. & Kearns, D.B. The cell biology of peritrichous flagella in Bacillus subtilis. Mol. Microbiol. 87, 211-229 (2013).
52. Bange, G., Petzold, G., Wild, K., Parlitz, R.O. & Sinning, I. The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP. Proc. Natl. Acad. Sci. USA 104, 13621-13625 (2007).
53. Lutkenhaus, J. & Sundaramoorthy, M. MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation. Mol. Microbiol. 48, 295-303 (2003).
54. Daumke, O., Weyand, M., Chakrabarti, P.P., Vetter, I.R. & Wittinghofer, A. The GTPase-activating protein Rap1GAP uses a catalytic asparagine. Nature 429, 197-201 (2004).
55. Bange, G., Wild, K. & Sinning, I. Protein translocation: checkpoint role for SRP GTPase activation. Curr. Biol. 17, R980-R982 (2007).
56. Leonard, T.A., Butler, P.J. & Lowe, J. Bacterial chromosome segregation: structure and DNA binding of the Soj dimer-a conserved biological switch. EMBO J. 24, 270-282 (2005).
57. Lutkenhaus, J. The ParA/MinD family puts things in their place. Trends Microbiol. 20, 411-418 (2012).