Monitoring calcium-induced conformational changes in recoverin by electrospray mass spectrometry

Protein Science

Volumn 6, Issue 4, 1997, Pages 843-850

  Neubert, Thomas A ^a,b,c   Walsh, Kenneth A ^a   Hurley, James B ^a,b   Johnson, Richard S ^a,d  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

^c Fournier Pharma GmbH   (Germany)

^d AMGEN INC   (United States)

Author keywords

calcium binding; hydrogen isotope exchange; mass spectrometry; N acylation; protein dynamics; recoverin

Indexed keywords

CALCIUM BINDING PROTEIN; RECOVERIN; RHODOPSIN;

ACYLATION; ARTICLE; BINDING SITE; CALCIUM BINDING; CONFORMATIONAL TRANSITION; HYDROGEN BOND; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

EID: 0030907866     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060411     Document Type: Article

References (35)

1. Ames JB, Porumb T, Tanaka T, Ikura M, Stryer L. 1995a. Amino-terminal myristoylation induces cooperative calcium binding to recoverin. J Biol Chem 270:4526-4533.
2. Ames JB, Tanaka T, Ikura M, Stryer L. 1995b. Nuclear magnetic resonance evidence for calcium-induced extrusion of the myristoyl group of recoverin. J Biol Chem 270:30909-30913.
3. Ames JB, Tanaka T, Stryer L, Ikura M. 1994. Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: Implications for the calcium-myristoyl switch. Biochemistry 33:10743-10753.
4. Biemann K. 1990. Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation. Methods Enzymol 193:455-479.
5. Chen CK, Inglese J, Lefkowitz RJ, Hurley JB. 1995. Ca++ dependent interaction of recoverin with rhodopsin kinase. J Biol Chem 270:18060-18066.
6. Covey TR, Huang EC, Henion JD. 1991. Structural characterization of protein tryptic peptides via liquid chromatography/mass spectrometry and collision-induced dissociation of their doubly charged molecular ions. Anal Chem 63:1193-1200.
7. Dizhoor AM, Chen CK, Olshevskaya E, Sinelnikova VV, Phillipov P, Hurley JB. 1993. Role of the acylated amino terminus of recoverin in calcium-dependent membrane interaction. Science 259:829-832.
8. 2 terminus of retinal recoverin is acylated by a small family of fatty acids. J Biol Chem 267:16033-16036.
9. Englander SW, Kallenbach NR. 1984. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Quart Rev Biophys 16:521-655.
10. Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. 1989. Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64-71.
11. Flaherty KM, Zozulya S, Stryer L, McKay DB. 1993. Three-dimensional structure of recoverin, a calcium sensor in vision. Cell 75:709-716.
12. Gray-Keller MP, Polans AS, Palczewski K, Detwiler PB. 1993. The effect of recoverin-like calcium-binding proteins on the photoresponse of retinal rods. Neuron 10:523-531.
13. Griko YV, Privalov PL, Venyaminov SY, Kutyshenko VP. 1988. Thermodynamic study of apomyoglobin structure. J Mol Biol 202:127-138.
14. Hughes RE, Brzovic PS, Klevit RE, Hurley JB. 1995. Calcium-dependent solvation of the myristoyl group of recoverin. Biochemistry 34:11410-11416.
15. Hunt DF, Yates JR, Shabanowitz J, Winston S, Hauer CR. 1986. Protein sequencing by tandem mass spectrometry. Proc Natl Acad Sci USA 83:6233-6237.
16. Johnson RS. 1996. Mass spectrometric measurements of changes in protein hydrogen exchange rates resulting from point mutations. J Am Soc Mass Spectrom 7:515-521.
17. Johnson RS, Ohguro H, Palczewski K, Hurley JB, Walsh KA, Neubert TA. 1994. Heterogeneous N-acylation is a tissue-and species-specific posttranslational modification. J Biol Chem 269:21067-21071.
18. Johnson RS, Walsh KA. 1994. Mass spectrometric measurement of protein amide hydrogen exchange rates of apo-and holo-myoglobin. Protein Sci 3:2411-2418.
19. Kataoka M, Mihara K, Tokunaga F. 1993. Recoverin alters its surface properties depending on both calcium-binding and N-terminal myristoylation. J Biochem (Tokyo) 114:535-540.
20. Katta V, Chait BT. 1993. Hydrogen/deuterium exchange electrospray ionization mass spectrometry: A method for probing protein conformational changes in solution. J Am Chem Soc 115:6317-6321.
21. Kawamura S. 1993. Rhodopsin phosphorylation as a mechanism of cyclic GMP phosphodiesterase regulation by S-modulin. Nature 362:855-857.
22. Kokame K, Fukada Y, Yoshizawa T, Takao T, Shimonishi Y. 1992. Novel lipid modification at the N-terminus of photoreceptor G protein alpha-subunit. Nature 359:749-752.
23. Liu Y, Smith DL. 1994. Probing high order structure of proteins by fast-atom bombardment mass spectrometry. J Am Soc Mass Spectrom 5:19-28.
24. Moncrief ND, Kretsinger RH, Goodman M. 1990. Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences. J Mol Evol 30:522-562.
25. Neubert TA, Johnson RS, Hurley JB, Walsh KA. 1992. The rod transducin alpha subunit amino terminus is heterogeneously fatty acylated. J Biol Chem 267:18274-18277.
26. Palczewski K, Subbaraya I, Gorczyca WA, Helekar BS, Ruiz CC, Ohguro H, Huang J, Zhao X, Crabb JW, Johnson RS, Walsh KA, Gray-Keller MP, Detwiler PB, Baehr W. 1994. Molecular cloning and characterization of retinal photoreceptor guanylyl cyclase activating protein (GCAP). Neuron 13:395-404.
27. Ray S, Zozulya S, Niemi GA, Flaherty KM, Brolley D, Dizhoor AM, McKay DB, Hurley J, Stryer L. 1992. Cloning, expression, and crystallization of recoverin, a calcium sensor in vision. Proc Natl Acad Sci USA 89:5705-5709.
28. Sanada K, Kokame K, Yoshizawa T, Takao T, Shimonishi Y, Fukada Y. 1995. Role of heterogeneous N-terminal acylation of recoverin in rhodopsin phosphorylation. J Biol Chem 270:15459-15462.
29. Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M. 1995. Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature 376:444-446.
30. Taylor JA, Walsh KA, Johnson RS. 1996. Sherpa: A Macintosh based expert system for the interpretation of ESI LC/MS and MS/MS of protein digests. Rapid Commun Mass Spectrom 10:679-687.
31. Teng DH, Chen CK, Hurley JB. 1994. A highly conserved homologue of bovine neurocalcin in Drosophila melanogaster is a Ca++ binding protein expressed in neuronal tissues. J Biol Chem 269:31900-31907.
32. Woodward C, Simon I, Tuchsen E. 1982. Hydrogen exchange and the dynamic structure of proteins. Mol Cell Biochem 48:135-160.
33. Zhang Z, Post CB, Smith DL. 1996. Amide hydrogen exchange determined by mass spectrometry: Application to rabbit muscle aldolase. Biochemistry 35:779-791.
34. Zhang Z, Smith DL. 1993. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci 2:522-531.
35. Zozulya S, Stryer L. 1992. Calcium-myristoyl protein switch. Proc Natl Acad Sci USA 89:11569-11573.