Inhibition of membrane-associated methyltransferases by a cholesterol-based metal chelator

Bioconjugate Chemistry

Volumn 16, Issue 3, 2005, Pages 490-493

  Hodges, Heather B ^a   Zhou, Mingkang ^a   Haldar, Saubhik ^a   Anderson, Jessica L ^a   Thompson, David H ^a   Hrycyna, Christine A ^a  

^a PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; CHELATION; ENZYMES; METALS;

CHELATING COMPOUND; CHELATING GROUPS; HIGH AFFINITY; INTEGRAL MEMBRANE; ISOPRENYLCYSTEINE CARBOXYLMETHYLTRANSFERASE; METAL CHELATING; METAL CHELATOR; METHYLTRANSFERASES; NITRILOTRIACETIC ACID; SYNTHESISED;

CHOLESTEROL;

CHOLESTEROL; CYSTEINE; ISOPRENYLCYSTEINE CARBOXYMETHYLTRANSFERASE; LYSINE; MEMBRANE LIPID; MEMBRANE PROTEIN; METAL CHELATE; METHYLTRANSFERASE; NITRILOTRIACETIC ACID; UNCLASSIFIED DRUG;

ARTICLE; CELL MEMBRANE; CHELATION; HYDROPHOBICITY; IC 50; INHIBITION KINETICS; METAL BINDING; YEAST;

EID: 18844379164     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc050027d     Document Type: Article

References (28)

1. Schmitt, L., Dietrich, C., and Tampe, R. (1994) Synthesis and Characterization of Chelator-Lipids for Reversible Immobilization of Engineered Proteins at Self-Assembled Lipid Interfaces. J. Am. Chem. Soc. 116, 8485-8491.
2. Shnek, D. R., Pack, D. W., Sasaki, D. Y., and Arnold, F. H. (1994) Specific Protein Attachment to Artificial Membranes via Coordination to Lipid-Bound Copper(II). Langmuir 10, 2382-2388.
3. Gritsch, S., Neumaier, K, Schmitt, L., and Tampe, R. (1995) Engineered fusion molecules at chelator lipid interfaces imaged by reflection interference contrast microscopy (RICM). Biosens Bioelectron 10, 805-812.
4. Dietrich, C., Boscheinen, O., Scharf, K. D., Schmitt, L., and Tampe, R. (1996) Functional immobilization of a DNA-binding protein at a membrane interface via histidine tag and synthetic chelator lipids. Biochemistry 35, 1100-1105.
5. Dietrich, C., Schmitt, L., and Tampe, R. (1995) Molecular organization of histidine-tagged biomolecules at self-assembled lipid interfaces using a novel class of chelator lipids. Proc. Natl. Acad. Sci. U.S.A. 92, 9014-9018.
6. Busch, K., and Tampe, R. (2001) Single molecule research on surfaces: from analytics to construction and back. J. Biotechnol. 82, 3-24.
7. Levy, D., Mosser, G., Lambert, O., Moeck, G. S., Bald, D., and Rigaud, J. L. (1999) Two-dimensional crystallization on lipid layer: A successful approach for membrane proteins. J. Struct. Biol. 127, 44-52.
8. Kubalek, E. W., Le Grice, S. F., and Brown, P. O. (1994) Two-dimensional crystallization of histidine-tagged, HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid. J. Struct. Biol. 113, 117-123.
9. Barklis, E., McDermott, J., Wilkens, S., Schabtach, E., Schmid, M. F., Fuller, S., Karanjia, S., Love, Z., Jones, R., Rui, Y., Zhao, X., and Thompson, D. (1997) Structural analysis of membrane-bound retrovirus capsid proteins. EMBO J. 16, 1199-1213.
10. Chiu, W., Avila-Sakar, A. J., and Schmid, M. F. (1997) Electron crystallography of macromolecular periodic arrays on phospholipid monolayers. Adv. Biophys. 34, 161-172.
11. Kornberg, R. D., and Darst, S. A. (1991) Two-dimensional crystals of proteins on lipid layers. Curr. Op. Struct. Biol. 1, 642-646.
12. Uzgiris, E. E., and Kornberg, R. D. (1983) Two-dimensional crystallization technique for imaging macromolecules, with application to antigen-antibody-complement complexes. Nature 301, 125-129.
13. Bischler, N., Balavoine, F., Milkereit, P., Tschochner, H., Mioskowski, C., and Schultz, P. (1998) Specific interaction and two-dimensional crystallization of histidine tagged yeast RNA polymerase I on nickel-chelating lipids. Biophys. J. 74, 1522-1532.
14. Celia, H., Wilson-Kubalek, E., Milligan, R. A., and Teyton, L. (1999) Structure and function of a membrane-bound murine MHC class I molecule. Proc. Natl. Acad. Sci. U.S.A. 96, 5634-5639.
15. Venien-Bryan, C., Balavoine, F., Toussaint, B., Mioskowski, C., Hewat, E. A., Helme, B., and Vignais, P. M. (1997) Structural study of the response regulator HupR from Rhodobacter capsulatus. Electron microscopy of two-dimensional crystals on a nickel-chelating lipid. J. Mol. Biol. 274, 687-692.
16. Zhang, F. L., and Casey, P. J. (1996) Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65, 241-269.
17. Young, S. G., Ambroziak, P., Kim, E., and Clarke, S. (2000) in The Enzymes, 3rd ed.; pp 155-213, Academic Press, San Diego, CA.
18. Hrycyna, C. A., and Clarke, S. (1993) Modification of eukaryotic signaling proteins by C-terminal methylation reactions. Pharmacol. Ther. 59, 281-300.
19. Clarke, S. (1992) Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu. Rev. Biochem. 61, 355-386.
20. Desrosiers, R. R., Nguyen, Q. T., and Beliveau, R. (1999) The carboxyl methyltransferase modifying G proteins is a metalloenzyme. Biochem. Biophys. Res. Commun. 261, 790-797.
21. Anderson, J. L., Frase, H., Michaelis, S., and Hrycyna, C. A. (2005) Purification, functional reconstitution and characterization of the Saccharomyces Cerevisiae isoprenylcysteine carboxyl methyltransferase Ste14p. J. Biol. Chem. 280, 7336-7345.
22. Zhou, M. H., Haldar, S., Franses, J., Kim, J. M., and Thompson, D. H. (2005) Synthesis and self-assembly properties of acylated cyclodextrins and nitrilotriacetic acid (NTA)-modified ligands for interfacial protein crystallization. Supramol. Chem. 17, 101-111.
23. Hrycyna, C. A., Wait, S. J., Backlund, P. S., Jr., and Michaelis, S. (1995) Yeast STE14 methyltransferase, expressed as TrpE-STE14 fusion protein in Escherichia coli, for in vitro carboxylmethylation of prenylated polypeptides. Methods Enzymol. 250, 251-266.
24. Ota, I. M., and Clarke, S. (1989) Enzymatic methylation of 23-29-kDa bovine retinal rod outer segment membrane proteins. Evidence for methyl ester formation at carboxyl-terminal cysteinyl residues. J. Biol. Chem. 264, 12879-12884.
25. Stephenson, R. C., and Clarke, S. (1990) Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic farnesyl cysteine-containing peptide substrate. J. Biol. Chem. 265, 16248-16254.
26. Hrycyna, C. A., and Clarke, S. (1990) Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae. Mol. Cell Biol. 10, 5071-5076.
27. Dai, Q., Choy, E., Chiu, V., Romano, J., Slivka, S. R., Steitz, S. A., Michaelis, S., and Philips, M. R. (1998) Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum. J. Biol. Chem. 273, 15030-15034.
28. Hrycyna, C. A., Sapperstein, S. K., Clarke, S., and Michaelis, S. (1991) The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins. EMBO J. 10, 1699-1709.