Electrospray mass spectrometric investigation of the chaperone SecB

Protein Science

Volumn 5, Issue 3, 1996, Pages 488-494

  Smith, Virginia F ^a   Schwartz, Brenda L ^b,c   Randall, Linda L ^a   Smith, Richard D ^b  

^a WASHINGTON STATE UNIVERSITY   (United States)

^b PACIFIC NORTHWEST NATIONAL LABORATORY   (United States)

^c ROCHE BIOSCIENCE   (United States)

Author keywords

chaperone; electrospray mass spectrometry; noncovalent interactions; SecB

Indexed keywords

CHAPERONE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; COVALENT BOND; ENZYME CONFORMATION; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TRANSPORT;

EID: 0029988081     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050310     Document Type: Article

References (26)

1. Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB. 1994. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371:578-586.
2. Breukink E, Kusters R, deKruijff B. 1992. In vitro studies on the folding characteristics of the Escherichia coli precursor protein Pre-PhoE. Eur J Biochem 208:419-425.
3. Chowdhury SK, Katta V, Chait BT. 1990. Probing conformational changes in proteins by mass spectrometry. Rapid Commun Mass Spectrom 4:81.
4. Fasman GD, Park K, Randall LL. 1995. Chaperone SecB: Conformational changes demonstrated by circular dichroism. J Prot Chem 14:595-600.
5. Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. 1990. Electrospray ionization - Principles and practice. Mass Spectrom Rev 9:37-70.
6. Gale DC, Smith RD. 1993. Small-volume and low flow-rate electrospray ionization mass spectrometry of aqueous samples. Rapid Commun Mass Spectrom 7:1017-1021.
7. Hardy SJS, Randall LL. 1991. A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB. Science 251:439-443.
8. Holmgren A, Braenden CI. 1989. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature 342:248-251.
9. Kraus E, Kiltz HH, Femfert UF. 1976. The specificity of proteinase K against oxidized insulin B chain. Hoppe Seyler's Z Physiol Chem 357:233-237.
10. Kumamoto CA, Chen L, Fandl J, Tai PC. 1989. Purification of the Escherichia coli secB gene product and demonstration of its activity in an in vitro protein translocation system. J Biol Chem 264:2242-2249.
11. Kumamoto CA, Nault AK. 1989. Characterization of the Escherichia coli protein export gene secB. Gene 75:167-175.
12. Light-Wahl KJ, Schwartz BL, Smith RD. 1994. Observation of the noncovalent quaternary associations of proteins by electrospray ionization mass spectrometry. J Am Chem Soc 116:5271-5278.
13. Loo JA, Udseth HR, Smith RD. 1988. Peptide and protein analysts by electrospray ionization-mass spectrometry and capillary electrophoresis-mass spectrometry. Rapid Commun Mass Spectrom 2:207-210.
14. Morshauser RC, Wang H, Flynn GC, Zuiderweg ERP. 1995. The peptide-binding domain of the chaperone protein Hsc 70 has an unusual secondary structure topology. Biochemistry 34:6261-6266.
15. Randall LL. 1992. Peptide binding by chaperone SecB: Implications for recognition of non-native structure. Science 257:241-245.
16. Randall LL, Hardy SJS. 1995. High selectivity with low specificity: How SecB solved the paradox of chaperone binding. Trends Biochem Sci 20. 65-69.
17. Rockwood AL, Busman M, Udseth HR, Smith RD. 1991. Thermally induced dissociation of ions from electrospray mass spectrometry. Rapid Commun Mass Spectrom 5:582-585.
18. Smith RD, Light-Wahl KJ. 1993. The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry: Promise, pitfalls and prognosis. Biol Mass Spectrom 22:493-501.
19. Smith RD, Loo JA, Barinaga CJ, Edmonds CG, Udseth HR. 1990a. Collisional activation and collision-activated dissociation of large multiply charged polypeptides and proteins produced by electrospray ionization. J Am Soc Mass Spectrom 1:53-65.
20. Smith RD, Loo JA, Edmonds CG, Barinaga CJ, Udseth HR. 1990b. New developments in biochemical mass spectrometry: Electrospray ionization. Anal Chem 62:882-889.
21. Szyperski T, Pellechia M, Wall D, Georgopoulous C, Wüthrich K. 1994. NMR structure determination of the Escherichia coli DNA J molecular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain. Proc Natl Acad Sci USA 91:11343-11347.
22. Topping TB, Randall LL. 1994. Determination of the binding frame within a physiological ligand for the chaperone SecB. Protein Sci 3:730-736.
23. Vrielink A, Beamer L, Le T, Eisenberg D. 1995. Crystallization of the chaperone SecB. Protein Sci 4:1651-1653.
24. Watanabe M, Blobel G. 1989. Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB. Proc Natl Acad Sci USA 86:2728-2732.
25. Weiss JB, Ray PH, Bassford PJ Jr. 1988. Purified SecB of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro. Proc Natl Acad Sci USA 85:8978-8982.
26. Winger BE, Light-Wahl KJ, Ogorzalek Loo RR, Udseth HR, Smith RD. 1993. Observation and implications of high mass-to-charge ratio ions from electrospray ionization mass spectrometry. J Am Soc Mass Spectrom 4:536-545.