The basis of asymmetry in the SecA:SecB complex

Journal of Molecular Biology

Volumn 427, Issue 4, 2015, Pages 887-900

  Suo, Yuying ^a   Hardy, Simon J S ^b   Randall, Linda L ^a  

^a University of Missouri   (United States)

^b UNIVERSITY OF YORK   (United Kingdom)

Author keywords

asymmetric binding; hybrid SecB species; protein interaction; Sec system; G stabilization

Indexed keywords

MONOMER; PROTEIN SECA; PROTEIN SECB; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; BACTERIAL SECRETION SYSTEM; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; SECA PROTEIN, BACTERIA; SECB PROTEIN, BACTERIA;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISULFIDE BOND; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; IN VITRO STUDY; ION EXCHANGE CHROMATOGRAPHY; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONTENT; PROTEIN CROSS LINKING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; PROTEIN STABILITY; STOICHIOMETRY; BACTERIAL SECRETION SYSTEM; CHEMICAL STRUCTURE; METABOLISM; PHYSIOLOGY; PROTEIN MULTIMERIZATION; PROTEIN TRANSPORT;

ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; BACTERIAL SECRETION SYSTEMS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION; PROTEIN TRANSPORT;

EID: 84922345092     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.12.008     Document Type: Article

References (22)

1. C. Mao, S.J.S. Hardy, and L.L. Randall Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA J Bacteriol 191 2009 978 984
2. L.L. Randall, and M.T. Henzl Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA Protein Sci 19 2010 1173 1179
3. Y. Suo, S.J.S. Hardy, and L.L. Randall Orientation of SecA and SecB in complex, derived from disulfide cross-linking J Bacteriol 193 2011 190 196
4. L.L. Randall, J.M. Crane, A.A. Lilly, G. Liu, C. Mao, and C.N. Patel Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export J Mol Biol 348 2005 479 489
5. Y. Tang, X. Pan, Y. Chen, P.C. Tai, and S.F. Sui Dimeric SecA couples the preprotein translocation in an asymmetric manner PLoS One 6 2011 e16498
6. D.B. Cooper, V.F. Smith, J.M. Crane, H.C. Roth, A.A. Lilly, and L.L. Randall SecA, the motor of the secretion machine, binds diverse partners on one interactive surface J Mol Biol 382 2008 74 87
7. T.B. Topping, R.L. Woodbury, D.L. Diamond, S.J.S. Hardy, and L.L. Randall Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibrium J Biol Chem 276 2001 7437 7441
8. P.M. Gannon, and C.A. Kumamoto Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein. [Erratum appears in J Biol Chem 1993 Jul 15;268(20):15324] J Biol Chem 268 1993 1590 1595
9. L.L. Randall, J.M. Crane, G. Liu, and S.J.S. Hardy Sites of interaction between SecA and the chaperone SecB, two proteins involved in export Protein Sci 13 2004 1124 1133
10. K.E. van Holde, and W.O. Weischet Boundary analysis of sedimentation velocity experiments with monodisperse and paucidisperse solutes Biopolymers 17 1978 1387 1403
11. B. Demeler, H. Saber, and J.C. Hansen Identification and interpretation of complexity in sedimentation velocity boundaries Biophys J 72 1997 397 407
12. R.L. Woodbury, S.J.S. Hardy, and L.L. Randall Complex behavior in solution of homodimeric SecA Protein Sci 11 2002 875 882
13. C.N. Patel, V.F. Smith, and L.L. Randall Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export Protein Sci 15 2006 1379 1386
14. J.M. Crane, C. Mao, A.A. Lilly, V.F. Smith, Y. Suo, and W.L. Hubbell 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 2005 295 307
15. J. Zhou, and Z. Xu Structural determinants of SecB recognition by SecA in bacterial protein translocation Nat Struct Biol 10 2003 942 947
16. J.F. Hunt, S. Weinkauf, L. Henry, J.J. Fak, P. McNicholas, and D.B. Oliver Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA Science 297 2002 2018 2026
17. L.L. Randall, T.B. Topping, D. Suciu, and S.J.S. Hardy Calorimetric analyses of the interaction between SecB and its ligands Protein Sci 7 1998 1195 1200
18. Z. Xu, J.D. Knafels, and K. Yoshino Crystal structure of the bacterial protein export chaperone secB Nat Struct Biol 7 2000 1172 1177
19. J.M. Crane, Y. Suo, A.A. Lilly, C. Mao, W.L. Hubbell, and L.L. Randall Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling J Mol Biol 363 2006 63 74
20. A.A. Lilly, J.M. Crane, and L.L. Randall Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands Protein Sci 18 2009 1860 1868
21. M.M. Haimann, Y. Akdogan, R. Philipp, R. Varadarajan, D. Hinderberger, and W.E. Trommer Conformational changes of the chaperone SecB upon binding to a model substrate - bovine pancreatic trypsin inhibitor (BPTI) Biol Chem 392 2011 849 858
22. C. Mao, C.E. Cheadle, S.J.S. Hardy, A.A. Lilly, Y. Suo, and R.R.S. Gari Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species Proc Natl Acad Sci USA 110 2013 11815 11820