Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export

Protein Science

Volumn 15, Issue 6, 2006, Pages 1379-1386

  Patel, Chetan N ^a,c   Smith, Virginia F ^b   Randall, Linda L ^a  

^a University of Missouri   (United States)

^b UNITED STATES NAVAL ACADEMY   (United States)

^c STANFORD UNIVERSITY   (United States)

Author keywords

Calorimetry; Export; Protein interactions; SecA; SecB

Indexed keywords

PROTEIN SECA; PROTEIN SECB;

ARTICLE; CALORIMETRY; CARBOXY TERMINAL SEQUENCE; ENTHALPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; STOICHIOMETRY; THERMODYNAMICS;

ADENOSINE TRIPHOSPHATASES; BACTERIAL PROTEINS; BINDING SITES; CALORIMETRY; MEMBRANE TRANSPORT PROTEINS; MULTIPROTEIN COMPLEXES; MUTATION; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 33744454411     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062141006     Document Type: Article

References (38)

1. Baud, C., Karamanou, S., Sianidis, G., Vrontou, E., Politou, A.S., and Economou, A. 2002. Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain. J. Biol. Chem. 277: 13724-13731.
2. Chervenak, M.C. and Toone, E.J. 1994. A direct measure of the contribution of solvent reorganization to the enthalpy of ligand binding. J. Am. Chem. Soc. 116: 10533-10539.
3. Chothia, C. and Janin, J. 1975. Principles of protein-protein recognition. Nature 256: 705-708.
4. Crane, J.M., Mao, C., Lilly, A.A., Smith, V.F., Suo, Y., Hubbell, W.L., and Randall, L.L. 2005. Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: Insight into the mechanism of ligand transfer during protein export. J. Mol. Biol. 353: 295-307.
5. de Keyzer, J., van der Sluis, E.O., Spelbrink, R.E., Nijstad, N., de Kruijff, B., Nouwen, N., van der Does, C., and Driessen, A.J. 2005. Covalently dimerized SecA is functional in protein translocation. J. Biol. Chem. 280: 35255-35260.
6. Fekkes, P., den Blaauwen, T., and Driessen, A.J. 1995. Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB. Biochemistry 34: 10078-10085.
7. Fekkes, P., de Wit, J.G., Boorsma, A., Friesen, R.H., and Driessen, A.J. 1999. Zinc stabilizes the SecB binding site of SecA. Biochemistry 38: 5111-5116.
8. Fukada, H. and Takahashi, K. 1998. Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride. Proteins 33: 159-166.
9. Grunwald, E. and Steel, C. 1995. Solvent reorganization and thermodynamic enthalpy-entropy compensation. J. Am. Chem. Soc. 117: 5687-5692.
10. Hardy, S.J.S. and Randall, L.L. 1991. A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB. Science 251: 439-443.
11. Hunt, J.F., Weinkauf, S., Henry, L., Fak, J.J., McNicholas, P., Oliver, D.B., and Deisenhofer, J. 2002. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Science 297: 2018-2026.
12. Jilaveanu, L.B. and Oliver, D. 2006. SecA dimer cross-linked at its subunit interface is functional for protein translocation. J. Bacteriol. 188: 335-338.
13. Jilaveanu, L.B., Zito, C.R., and Oliver, D. 2005. Dimeric SecA is essential for protein translocation. Proc. Natl. Acad. Sci. 102: 7511-7516.
14. Jones, S. and Thornton, J.M. 1995. Protein-protein interactions: A review of protein dimer structures. Prog. Biophys. Mol. Biol. 63: 31-59.
15. Khisty, V.J., Munske, G.R., and Randall, L.L. 1995. Mapping of the binding frame for the chaperone SecB within a natural ligand, galactose-binding protein. J. Biol. Chem. 270: 25920-25927.
16. Kimura, E., Akita, M., Matsuyama, S., and Mizushima, S. 1991. Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli. J. Biol. Chem. 266: 6600-6606.
17. Kourtz, L. and Oliver, D. 2000. Tyr-326 plays a critical role in controlling SecA-preprotein interaction. Mol. Microbiol. 37: 1342-1356.
18. Liu, L. and Guo, Q.X. 2001. Isokinetic relationship, isoequilibrium relationship, and enthalpy-entropy compensation. Chem. Rev. 101: 673-695.
19. Morin, P.E. and Freire, E. 1991. Direct calorimetric analysis of the enzymatic activity of yeast Cytochrome C Oxidase. Biochemistry 30: 8494-8500.
20. Or, E., Navon, A., and Rapoport, T. 2002. Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane. EMBO J. 21: 4470-4479.
21. Or, E., Boyd, D., Gon, S., Beckwith, J., and Rapoport, T. 2005. The bacterial ATPase SecA functions as a monomer in protein translocation. J. Biol. Chem. 280: 9097-9105.
22. Osborne, A.R., Clemons Jr., W.M., and Rapoport, T.A. 2004. A large conformational change of the translocation ATPase SecA. Proc. Natl. Acad. Sci. 101: 10937-10942.
23. Papanikou, E., Karamanou, S., Baud, C., Frank, M., Sianidis, G., Keramisanou, D., Kalodimos, C.G., Kuhn, A., and Economou, A. 2005. Identification of the preprotein binding domain of SecA. J. Biol. Chem. 280: 43209-43217.
24. Ramamurthy, V. and Oliver, D. 1997. Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding. J. Biol. Chem. 272: 23239-23246.
25. Randall, L.L. and Hardy, S.J.S. 1995. High selectivity with low specificity: How SecB has solved the paradox of chaperone binding. Trends Biochem. Sci. 20: 65-69.
26. Randall, L.L., Topping, T.B., Suciu, D., and Hardy, S.J.S. 1998. Calorimetric analyses of the interaction between SecB and its ligands. Protein Sci. 7: 1195-1200.
27. Randall, L.L., Crane, J.M., Liu, G., and Hardy, S.J.S. 2004. Sites of interaction between SecA and the chaperone SecB, two proteins involved in export. Protein Sci. 13: 1124-1133.
28. Randall, L.L., Crane, J.M., Lilly, A.A., Liu, G., Mao, C., Patel, C.N., and Hardy, S.J.S. 2005. Asymmetric binding between SecA and SecB two symmetric proteins: Implications for function in export. J. Mol. Biol. 348: 479-489.
29. Smith, V.F., Schwartz, B.L., Randall, L.L., and Smith, R.D. 1996. Electrospray mass spectrometric investigation of the chaperone SecB. Protein Sci. 5: 488-494.
30. Smith, V.F., Hardy, S.J.S., and Randall, L.L. 1997. Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein. Protein Sci. 6: 1746-1755.
31. Sola, M., Battistuzzi, G., and Borsari, M. 2005. Modulation of the free energy of reduction in metalloproteins. Chemtracts 18: 73-86.
32. Topping, T.B. and Randall, L.L. 1994. Determination of the binding frame within a physiological ligand for the chaperone SecB. Protein Sci. 3: 730-736.
33. Volkert, T.L., Baleja, J.D., and Kumamoto, C.A. 1999. A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB. Biochem. Biophys. Res. Commun. 264: 949-954.
34. Woodbury, R.L., Topping, T.B., Diamond, D.L., Suciu, D., Kumamoto, C.A., Hardy, S.J.S., and Randall, L.L. 2000. Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions. J. Biol. Chem. 275: 24191-24198.
35. Woodbury, R.L., Hardy, S.J.S., and Randall, L.L. 2002. Complex behavior in solution of homodimeric SecA. Protein Sci. 11: 875-882.
36. Xu, Z., Knafels, J.D., and Yoshino, K. 2000. Crystal structure of the bacterial protein export chaperone SecB. Nat. Struct. Biol. 7: 1172-1177.
37. Zhou, J. and Xu, Z. 2003. Structural determinants of SecB recognition by SecA in bacterial protein translocation. Nat. Struct. Biol. 10: 942-947.
38. Zhou, Z.S., Peariso, K., Penner-Hahn, J.E., and Matthews, R.G. 1999. Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli. Biochemistry 38: 15915-15926.