Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A

Journal of Biological Chemistry

Volumn 287, Issue 30, 2012, Pages 25589-25595

  Lim, Jung Chae ^a   Gruschus, James M ^a   Ghesquière, Bart ^a,b,c   Kim, Geumsoo ^a   Piszczek, Grzegorz ^a   Tjandra, Nico ^a   Levine, Rodney L ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^b GHENT UNIVERSITY   (Belgium)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT SYSTEMS; BIOPHYSICAL PROPERTIES; CYCLIC OXIDATION; CYTOSOLIC; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; MYRISTOYLATION; PROTEIN-PROTEIN INTERACTIONS; REACTIVE OXYGEN SPECIES; SOLUTION STRUCTURES; STRUCTURE FUNCTIONS;

ENZYMES; MAMMALS; PROTEINS;

AMINO ACIDS;

APOLIPOPROTEIN A1; GLYCINE; METHIONINE SULFOXIDE REDUCTASE A; MYRISTOYLATED METHIONINE SULFOXIDE REDUCTASE A; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME STRUCTURE; GEL PERMEATION CHROMATOGRAPHY; HYDROPHOBICITY; MOLECULAR WEIGHT; MOUSE; MYRISTYLATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS; THERMOSTABILITY; ULTRACENTRIFUGATION;

ANIMALS; LIPOYLATION; METHIONINE; METHIONINE SULFOXIDE REDUCTASES; MICE; PROTEIN STRUCTURE, TERTIARY;

EID: 84864095297     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.368936     Document Type: Article

References (30)

1. Stadtman, E. R., and Levine, R. L. (2006) in Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases (Dalle-Donne, I., Scaloni, A., and Butterfield, D. A., eds) pp. 3-23,Wiley Interscience, New York
2. Weissbach, H., Resnick, L., and Brot, N. (2005) Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. Biochim. Biophys. Acta 1703, 203-212 (Pubitemid 40170443)
3. Luo, S., and Levine, R. L. (2009) Methionine in proteins defends against oxidative stress. FASEB J. 23, 464-472
4. Lowther, W. T., Weissbach, H., Etienne, F., Brot, N., and Matthews, B. W. (2002) The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB. Nat. Struct. Biol. 9, 348-352 (Pubitemid 34462552)
5. Lim, J. C., You, Z., Kim, G., and Levine, R. L. (2011) Methionine sulfoxide reductase A is a stereospecific methionine oxidase. Proc. Natl. Acad. Sci. U.S.A. 108, 10472-10477
6. Kim, G., Cole, N. B., Lim, J. C., Zhao, H., and Levine, R. L. (2010) Dual sites of protein initiation control the localization and myristoylation of methionine sulfoxide reductase A. J. Biol. Chem. 285, 18085-18094
7. Resh, M. D. (1999) Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451, 1-16
8. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
9. Laue, T. M., Shad, B. D., Ridgeway, T. M., and Pelletier, S. L. (1992) in Analytical Ultracentrifugation in Biochemistry and Polymer Sciences (Harding, S. E., Rowe, A. J., and Horton, J. C. eds) pp. 90-125, Royal Society of Chemistry, Cambridge, UK
10. Lebowitz, J., Lewis, M. S., and Schuck, P. (2002) Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci. 11, 2067-2079 (Pubitemid 34919611)
11. Shen, Y., Delaglio, F., Cornilescu, G., and Bax, A. (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 213-223
12. Schwieters, C. D., Kuszewski, J. J., Tjandra, N., and Clore, G. M. (2003) The Xplor-NIH NMR molecular structure determination package. J. Magn. Reson. 160, 65-73
13. Folmer, R. H., Hilbers, C. W., Konings, R. N., and Nilges, M. (1997) Floating stereospecific assignment revisited: application to an 18-kDa protein and comparison with J-coupling data. J. Biomol. NMR 9, 245-258 (Pubitemid 127505386)
14. Zheng, J., Knighton, D. R., Xuong, N. H., Taylor, S. S., Sowadski, J. M., and Ten Eyck, L. F. (1993) Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. Protein Sci. 2, 1559-1573 (Pubitemid 23294335)
15. Ghesquiere, B., Jonckheere, V., Colaert, N., Van Durme, J., Timmerman, E., Goethals, M., Schymkowitz, J., Rousseau, F., Vandekerckhove, J., and Gevaert, K. (2011) Redox proteomics of protein-bound methionine oxidation. Mol. Cell. Proteomics 10, M110.006866
16. Liu, Y., Kahn, R. A., and Prestegard, J. H. (2009) Structure and membrane interaction of myristoylated ARF1. Structure 17, 79-87
17. 2+-induced extrusion of the myristoyl group of recoverin. J. Biol. Chem. 270, 30909-30913
18. Lowther, W. T., Brot, N., Weissbach, H., and Matthews, B. W. (2000) Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme. Biochemistry 39, 13307-13312
19. Pankhurst, G., Wang, X. L., Wilcken, D. E., Baernthaler, G., Panzenböck, U., Raftery, M., and Stocker, R. (2003) Characterization of specifically oxidized apolipoproteins in mildly oxidized high density lipoprotein. J. Lipid Res. 44, 349-355 (Pubitemid 37287778)
20. Wong, Y. Q., Binger, K. J., Howlett, G. J., and Griffin, M. D. (2010) Methionine oxidation induces amyloid fibril formation by full-length apolipoprotein A-I. Proc. Natl. Acad. Sci. U.S.A. 107, 1977-1982
21. Resh, M. D. (2006) Trafficking and signaling by fatty-acylated and prenylated proteins. Nat. Chem. Biol. 2, 584-590
22. Zhao, H., Kim, G., Liu, C., and Levine, R. L. (2010) Transgenic mice overexpressing methionine sulfoxide reductase A: characterization of embryonic fibroblasts. Free Radic. Biol. Med. 49, 641-648
23. Cole, N. B., Daniels, M. P., Levine, R. L., and Kim, G. (2010) Oxidative stress causes reversible changes in mitochondrial permeability and structure. Exp. Gerontol. 45, 596-602
24. Zhao, H., Sun, J., Deschamps, A. M., Kim, G., Liu, C., Murphy, E., and Levine, R. L. (2011) Myristoylated methionine sulfoxide reductase A protects the heart from ischemia-reperfusion injury. Am. J. Physiol. Heart Circ. Physiol. 301, H1513-1518
25. Tang, C., Loeliger, E., Luncsford, P., Kinde, I., Beckett, D., and Summers, M. F. (2004) Entropic switch regulates myristate exposure in the HIV-1 matrix protein. Proc. Natl. Acad. Sci. U.S.A. 101, 517-522 (Pubitemid 38084668)
26. Gaffarogullari, E. C., Masterson, L. R., Metcalfe, E. E., Traaseth, N. J., Balatri, E., Musa, M. M., Mullen, D., Distefano, M. D., and Veglia, G. (2011) A myristoyl/phosphoserine switch controls cAMP-dependent protein kinase association to membranes. J. Mol. Biol. 411, 823-836
27. Morgan, C. R., Miglionico, B. V., and Engen, J. R. (2011) Effects of HIV-1 Nef on human N-myristoyltransferase 1. Biochemistry 50, 3394-3403
28. Losonczi, J. A., and Prestegard, J. H. (1998) Nuclear magnetic resonance characterization of the myristoylated, N-terminal fragment of ADP-ribosylation factor 1 in a magnetically oriented membrane array. Biochemistry 37, 706-716 (Pubitemid 28123806)
29. Amor, J. C., Horton, J. R., Zhu, X., Wang, Y., Sullards, C., Ringe, D., Cheng, X., and Kahn, R. A. (2001) Structures of Yeast ARF2 and ARL1. J. Biol. Chem. 276, 42477-42484
30. Levine, R. L., Mosoni, L., Berlett, B. S., and Stadtman, E. R. (1996) Methionine residues as endogenous antioxidants in proteins. Proc. Natl. Acad. Sci. U.S.A. 93, 15036-15040 (Pubitemid 27009547)