Nucleotide-binding characteristics of human guanylate-binding protein 1 (hGBP1) and identification of the third GTP-binding motif

Journal of Molecular Biology

Volumn 292, Issue 2, 1999, Pages 321-332

  Praefcke, Gerrit J K ^a   Geyer, Matthias ^b   Schwemmle, Martin ^c   Robert Kalbitzer, Hans ^b   Herrmann, Christian ^a  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^b MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

^c UNIVERSITY OF FREIBURG   (Germany)

Author keywords

Aluminium fluoride; GTP binding protein; Interferon; Kinetics; Titration

Indexed keywords

ALUMINUM FLUORIDE; GUANINE NUCLEOTIDE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE PHOSPHATE; GUANOSINE TRIPHOSPHATE; MUTANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING KINETICS; BINDING SITE; CALORIMETRY; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; FLUOROMETRY; HUMAN; HYDROLYSIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN NUCLEIC ACID INTERACTION;

EID: 0033578805     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3062     Document Type: Article

References (50)

1. Anderson S. L., Carton J. M., Luo J., Xing L., Rubin B. Y. Interferon-induced guanylate binding protein-1 (GBP-1). mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus. Virology. 256:1999;8-14.
2. Asundi V. K., Stahl R. C., Showalter L., Conner K. J., Carey D. J. Molecular cloning and characterization of an isoprenylated 67 kDa protein. Biochim. Biophys. Acta. 1217:1994;257-265.
3. Cheng Y. S., Patterson C. E., Staeheli P. Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP. Mol. Cell. Biol. 11:1991;4717-4725.
4. iα1and the mechanism of GTP hydrolysis. Science. 265:1994;1405-1412.
5. Dever T. E., Glynias M. J., Merrick W. C. GTP-binding domain: three consensus sequence elements with distinct spacing. Proc. Natl Acad. Sci. USA. 84:1987;1814-1818.
6. Gill S. C., von Hippel P. H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
7. sαin Escherichia coli. Purification and properties of two forms of the protein. J. Biol. Chem. 264:1989;409-418.
8. Han B. H., Park D. J., Lim R. W., Im J. H., Kim H. D. Cloning, expression, and characterization of a novel guanylate-binding protein, GBP3 in murine erythroid progenitor cells. Biochim. Biophys. Acta. 1384:1998;373-386.
9. Herrmann C., Nassar N. Ras and its effectors. Prog. Biophys. Mol. Biol. 66:1996;1-41.
10. 31P NMP spectroscopy of G protein α subunits. J. Biol. Chem. 266:1991;3396-3401.
11. Hoffmann G. R., Nassar N., Oswald R. E., Cerione R. A. Fluoride activation of the Rho family GTP-binding protein Cdc42Hs. J. Biol. Chem. 273:1998;4392-4399.
12. IUPAC. Recommendations for the presentation of NMR structures of proteins and nucleic acids. Pure Appl. Chem. 70:1998;117-142.
13. John J., Sohmen R., Feuerstein J., Linke R., Wittinghofer A., Goody R. S. Kinetics of interaction of nucleotides with nucleotide-free H-ras p21. Biochemistry. 29:1990;6058-6065.
14. Kang C., Sun N., Honzatko R. B., Fromm H. J. Replacement of Asp333 with Asn by site-directed mutagenesis changes the substrate specificity of Escherichia coli adenylosuccinate synthetase from guanosine 5′-triphosphate to xanthosine 5′-triphosphate. J. Biol. Chem. 269:1994;24046-24049.
15. Kjeldgaard M., Nyborg J. Refined structure of elongation factor EF-Tu from Escherichia coli. J. Mol. Biol. 223:1992;721-742.
16. Klebe C., Nishimoto T., Wittinghofer F. Functional expression in Escherichia coli of the mitotic regulator proteins p24ran and p45rcc1 and fluorescence measurements of their interaction. Biochemistry. 32:1993;11923-11928.
17. Landis H., Simon-Jödicke A., Klöti A., Di Paolo C., Schnorr J.-J., Schneider-Schaulies S., Hefti H. P., Pavlovic J. Human MxA protein confers resistance to Semliki forest virus and inhibits the amplification of a Semliki forest virus-based replicon in the absence of viral structural proteins. J. Virol. 72:1998;1516-1522.
18. Lenzen C., Cool R. H., Wittinghofer A. Analysis of intrinsic and CDC25-stimulated guanine nucleotide exchange of p21ras-nucleotide complexes by fluorescence measurements. Methods Enzymol. 255:1995;95-109.
19. iαafter expression in Escherichia coli. J. Biol. Chem. 265:1990;8243-8251.
20. 19F NMR. J. Biol. Chem. 268:1993;7093-7100.
21. 19F NMR spectra. J. Magn. Reson. B113:1996;177-178.
22. McNiven M. A. Dynamin: a molecular motor with pinchase action. Cell. 94:1998;151-154.
23. Mélen K., Ronni T., Lotta T., Julkunen I. Enzymatic characterization of interferon-induced antiviral GTPases murine Mx1 and human MxA proteins. J. Biol. Chem. 269:1994;2009-2015.
24. Mittal R., Ahmadian M. R., Goody R. S., Wittinghofer A. Formation of a transition-state analog of the Ras GTPase reaction by Ras·GDP, tetrafluoroaluminate, and GTPase-activating proteins. Science. 273:1996;115-117.
25. Nantais D. E., Schwemmle M., Stickney J. T., Vestal D. J., Buss J. E. Prenylation of an interferon-γ-induced GTP-binding protein: the human guanylate binding protein, huGBP1. J. Leuk. Biol. 60:1996;423-431.
26. Nelson D. J., Martin R. B. Speciation in systems containing aluminum, nucleoside diphosphates, and fluoride. J. Inorg. Biochem. 43:1991;37-43.
27. Noel J. P., Hamm H. E., Sigler P. B. The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature. 366:1993;654-663.
28. Pai E. F., Krengel U., Petsko G. A., Goody R. S., Kabsch W., Wittinghofer A. Refined crystal structure of the triphosphate conformation of H- ras p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis. EMBO J. 9:1990;2351-2359.
29. Pavlovic J., Arzet H. A., Hefti H. P., Frese M., Rost D., Ernst B., Kolb E., Staeheli P., Haller O. Enhanced virus resistance of transgenic mice expressing the human MxA protein. J. Virol. 69:1995;4506-4510.
30. Pitossi F., Blank A., Schröder A., Schwarz A., Hüssi P., Schwemmle M., Pavlovic J., Staeheli P. A functional GTP-binding motif is necessary for antiviral activity of Mx proteins. J. Virol. 67:1993;6726-6732.
31. Richter M. F., Schwemmle M., Herrmann C., Wittinghofer A., Staeheli P. Interferon-induced MxA protein. GTP binding and GTP hydrolysis properties. J. Biol. Chem. 270:1995;13512-13517.
32. Rittinger K., Walker P. A., Eccleston J. F., Smerdon S. J., Gamblin S. J. Structure at 1.65 angstrom of RhoA and its GTPase-activating protein in complex with a transition state analogue. Nature. 389:1997;758-762.
33. Scheffzek K., Ahmadian M. R., Kabsch W., Wiesmüller L., Lautwein A., Schmitz F., Wittinghofer A. The Ras-RasGAP complex: Structural basis for activation and its loss in oncogenic Ras mutants. Science. 277:1997;333-338.
34. xphosphoryl transfer transition state analog. Nature Struct. Biol. 6:1999;721-723.
35. Schmidt G., Lenzen C., Simon I., Deuter R., Cool R. H., Goody R. S., Wittinghofer A. Biochemical and biological consequences of changing the specificity of p21ras from guanosine to xanthosine nucleotides. Oncogene. 12:1996;87-96.
36. Schwemmle M., Staeheli P. The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP. J. Biol. Chem. 269:1994;11299-11305.
37. Schwemmle M., Weining K. C., Richter M. F., Schumacher B., Staeheli P. Vesicular stomatitis virus transcription inhibited by purified MxA protein. Virology. 206:1995;545-554.
38. Schwemmle M., Kaspers B., Irion A., Staeheli P., Schultz U. Chicken guanylate-binding protein-conservation of GTPase activity and induction by cytokines. J. Biol. Chem. 271:1996;10304-10308.
39. Sever S., Muhlberg A. B., Schmid S. L. Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis. Nature. 398:1999;481-486.
40. Simon I., Zerial M., Goody R. S. Kinetics of interaction of Rab5 and Rab7 with nucleotides and Magnesium ions. J. Biol. Chem. 271:1996;20470-20478.
41. -. Nature. 372:1994;276-279.
42. Staeheli P., Haller O., Boll W., Lindenmann J., Weissmann C. Mx protein: constitutive expression in 3T3 cells transformed with cloned Mx cDNA confers selective resistance to influenza virus. Cell. 44:1986;147-158.
43. Strehlow I., Lohmann-Matther M.-L., Decker T. The interferon-inducible GBP1 gene: structure and mapping to human chromosome 1. Gene. 144:1994;295-299.
44. Vestal D. J., Buss J. E., McKercher S. R., Jenkins N. A., Copeland N. G., Kelner G. S., Asundi V. K., Maki R. A. Murine GBP-2: A new IFN-γ-induced member of the GBP family of GTPases isolated from macrophages. J. Interferon Cytokine Res. 18:1998;977-985.
45. 3+, and fluoride. J. Inorg. Biochem. 58:1995;29-47.
46. Warnock D. E., Schmid S. L. Dynamin GTPase, a force-generating molecular switch. Bio- Essays. 18:1996;885-893.
47. Weijland A., Parlato G., Parmeggiani A. Elongation factor Tu D138N, a mutant with modified substrate specificity, as a tool to study energy consumption in protein biosynthesis. Biochemistry. 33:1994;10711-10717.
48. Wiseman T., Williston S., Brandts J. F., Lin L.-N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179:1989;131-137.
49. Wynn T. A., Nicolet C. M., Paulnock D. M. Identification and characterization of a new gene family induced during macrophage activation. J. Immunol. 147:1991;4384-4392.
50. o-mutant that binds xanthine nucleotides. J. Biol. Chem. 272:1997;18015-18019.