메뉴 건너뛰기




Volumn 289, Issue 1, 2014, Pages 476-484

Nitric oxide activation of guanylate cyclase pushes the α1 signaling helix and the β1 heme-binding domain closer to the substrate-binding site

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ACTIVATION; FORSTER RESONANCE ENERGY TRANSFER; NITRIC OXIDE; PORPHYRINS;

EID: 84891692632     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.504472     Document Type: Article
Times cited : (21)

References (34)
  • 1
    • 79956211294 scopus 로고    scopus 로고
    • Structure, signaling mechanism and regulation of the natriuretic peptide receptor guanylate cyclase
    • Misono, K. S., Philo, J. S., Arakawa, T., Ogata, C. M., Qiu, Y., Ogawa, H., and Young, H. S. (2011) Structure, signaling mechanism and regulation of the natriuretic peptide receptor guanylate cyclase. FEBS J. 278, 1818-1829
    • (2011) FEBS J. , vol.278 , pp. 1818-1829
    • Misono, K.S.1    Philo, J.S.2    Arakawa, T.3    Ogata, C.M.4    Qiu, Y.5    Ogawa, H.6    Young, H.S.7
  • 2
    • 84861857184 scopus 로고    scopus 로고
    • Structure and regulation of soluble guanylate cyclase
    • Derbyshire, E. R., and Marletta, M. A. (2012) Structure and regulation of soluble guanylate cyclase. Annu. Rev. Biochem. 81, 533-559
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 533-559
    • Derbyshire, E.R.1    Marletta, M.A.2
  • 3
    • 3142582002 scopus 로고    scopus 로고
    • Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain. Rotation mechanism for transmembrane signal transduction
    • DOI 10.1074/jbc.M313222200
    • Ogawa, H., Qiu, Y., Ogata, C. M., and Misono, K. S. (2004) Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction. J. Biol. Chem. 279, 28625-28631 (Pubitemid 38900145)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28625-28631
    • Ogawa, H.1    Qiu, Y.2    Ogata, C.M.3    Misono, K.S.4
  • 4
    • 7044233148 scopus 로고    scopus 로고
    • Structural insights into the regulation and the activation mechanism of mammalian guanylyl cyclases
    • DOI 10.1016/j.pharmthera.2004.08.003, PII S0163725804001081
    • Padayatti, P. S., Pattanaik, P., Ma, X., and Van Den Akker, F. (2004) Structural insights into the regulation and the activation mechanism of mammalian guanylyl cyclases. Pharmacol. Ther. 104, 83-99 (Pubitemid 39424255)
    • (2004) Pharmacology and Therapeutics , vol.104 , Issue.2 , pp. 83-99
    • Padayatti, P.S.1    Pattanaik, P.2    Ma, X.3    Van Den Akker, F.4
  • 5
    • 14844344676 scopus 로고    scopus 로고
    • Expression and characterization of the catalytic domains of soluble guanylate cyclase: Interaction with the heme domain
    • DOI 10.1021/bi047601d
    • Winger, J. A., and Marletta, M. A. (2005) Expression and characterization of the catalytic domains of soluble guanylate cyclase: interaction with the heme domain. Biochemistry 44, 4083-4090 (Pubitemid 40358061)
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 4083-4090
    • Winger, J.A.1    Marletta, M.A.2
  • 6
    • 77955402749 scopus 로고    scopus 로고
    • Fluorescent fusion proteins of soluble guanylyl cyclase indicate proximity of the heme nitric oxide domain and catalytic domain
    • Haase, T., Haase, N., Kraehling, J. R., and Behrends, S. (2010) Fluorescent fusion proteins of soluble guanylyl cyclase indicate proximity of the heme nitric oxide domain and catalytic domain. PLoS One 5, e11617
    • (2010) PLoS One , vol.5
    • Haase, T.1    Haase, N.2    Kraehling, J.R.3    Behrends, S.4
  • 7
    • 2442506761 scopus 로고    scopus 로고
    • Differential inhibition of adenylyl cyclase isoforms and soluble guanylyl cyclase by purine and pyrimidine nucleotides
    • DOI 10.1074/jbc.M312560200
    • Gille, A., Lushington, G. H., Mou, T. C., Doughty, M. B., Johnson, R. A., and Seifert, R. (2004) Differential inhibition of adenylyl cyclase isoforms and soluble guanylyl cyclase by purine and pyrimidine nucleotides. J. Biol. Chem. 279, 19955-19969 (Pubitemid 38623438)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 19955-19969
    • Gille, A.1    Lushington, G.H.2    Mou, T.-C.3    Doughty, M.B.4    Johnson, R.A.5    Seifert, R.6
  • 8
    • 0037630420 scopus 로고    scopus 로고
    • 2′(3′)-O-(N-methylanthraniloyl)-substituted GTP analogs: A novel class of potent competitive adenylyl cyclase inhibitors
    • DOI 10.1074/jbc.M211292200
    • Gille, A., and Seifert, R. (2003) 2' (3')-O-(N-methylanthraniloyl)- substituted GTP analogs: a novel class of potent competitive adenylyl cyclase inhibitors. J. Biol. Chem. 278, 12672-12679 (Pubitemid 36800027)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 12672-12679
    • Gille, A.1    Seifert, R.2
  • 9
    • 77953083424 scopus 로고    scopus 로고
    • A real time fluorescent assay of the purified nitric oxide receptor, guanylyl cyclase
    • Newton, M., Niewczas, I., Clark, J., and Bellamy, T. C. (2010) A real time fluorescent assay of the purified nitric oxide receptor, guanylyl cyclase. Anal. Biochem. 402, 129-136
    • (2010) Anal. Biochem. , vol.402 , pp. 129-136
    • Newton, M.1    Niewczas, I.2    Clark, J.3    Bellamy, T.C.4
  • 10
    • 34548315751 scopus 로고    scopus 로고
    • Molecular analysis of the interaction of Bordetella pertussis adenylyl cyclase with fluorescent nucleotides
    • DOI 10.1124/mol.107.034413
    • Göttle, M., Dove, S., Steindel, P., Shen, Y., Tang, W. J., Geduhn, J., König, B., and Seifert, R. (2007) Molecular analysis of the interaction of Bordetella pertussis adenylyl cyclase with fluorescent nucleotides. Mol. Pharmacol. 72, 526-535 (Pubitemid 47347287)
    • (2007) Molecular Pharmacology , vol.72 , Issue.3 , pp. 526-535
    • Gottle, M.1    Dove, S.2    Steindel, P.3    Shen, Y.4    Tang, W.-J.5    Geduhn, J.6    Konig, B.7    Seifert, R.8
  • 11
    • 14844299755 scopus 로고    scopus 로고
    • Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2′(3′)-O-(N-methylanthraniloyl)-guanosine 5′-triphosphate
    • DOI 10.1074/jbc.M409076200
    • Mou, T. C., Gille, A., Fancy, D. A., Seifert, R., and Sprang, S. R. (2005) Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2' (3')-O-(N-methylanthraniloyl)-guanosine 5'-triphosphate. J. Biol. Chem. 280, 7253-7261 (Pubitemid 40341283)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 7253-7261
    • Mou, T.-C.1    Gille, A.2    Fancy, D.A.3    Seifert, R.4    Sprang, S.R.5
  • 12
    • 33747624168 scopus 로고    scopus 로고
    • Broad specificity of mammalian adenylyl cyclase for interaction with 2′,3′-substituted purine- and pyrimidine nucleotide inhibitors
    • DOI 10.1124/mol.106.026427
    • Mou, T. C., Gille, A., Suryanarayana, S., Richter, M., Seifert, R., and Sprang, S. R. (2006) Broad specificity of mammalian adenylyl cyclase for interaction with 2', 3'-substituted purine and pyrimidine nucleotide inhibitors. Mol. Pharmacol. 70, 878-886 (Pubitemid 44268445)
    • (2006) Molecular Pharmacology , vol.70 , Issue.3 , pp. 878-886
    • Mou, T.-C.1    Gille, A.2    Suryanarayana, S.3    Richter, M.4    Seifert, R.5    Sprang, S.R.6
  • 13
    • 0034571242 scopus 로고    scopus 로고
    • Cloning and functional expression of the rat α (2) subunit of soluble guanylyl cyclase
    • Koglin, M., and Behrends, S. (2000) Cloning and functional expression of the rat α (2) subunit of soluble guanylyl cyclase. Biochim. Biophys. Acta. 1494, 286-289
    • (2000) Biochim. Biophys. Acta. , vol.1494 , pp. 286-289
    • Koglin, M.1    Behrends, S.2
  • 14
    • 77957906338 scopus 로고    scopus 로고
    • Direct fusion of subunits of heterodimeric nitric oxide sensitive guanylyl cyclase leads to functional enzymes with preserved biochemical properties: Evidence for isoform specific activation by ciguates
    • Haase, N., Haase, T., Kraehling, J. R., and Behrends, S. (2010) Direct fusion of subunits of heterodimeric nitric oxide sensitive guanylyl cyclase leads to functional enzymes with preserved biochemical properties: evidence for isoform specific activation by ciguates. Biochem. Pharmacol. 80, 1676-1683
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 1676-1683
    • Haase, N.1    Haase, T.2    Kraehling, J.R.3    Behrends, S.4
  • 15
    • 80053585971 scopus 로고    scopus 로고
    • The amino-terminus of nitric oxide sensitive guanylyl cyclase alpha (1) does not affect dimerization but influences subcellular localization
    • Kraehling, J. R., Busker, M., Haase, T., Haase, N., Koglin, M., Linnenbaum, M., and Behrends, S. (2011) The amino-terminus of nitric oxide sensitive guanylyl cyclase alpha (1) does not affect dimerization but influences subcellular localization. PLoS One 6, e25772
    • (2011) PLoS One , vol.6
    • Kraehling, J.R.1    Busker, M.2    Haase, T.3    Haase, N.4    Koglin, M.5    Linnenbaum, M.6    Behrends, S.7
  • 16
    • 0002557253 scopus 로고    scopus 로고
    • Calibration of fluorescence resonance energy transfer in microscopy using genetically engineered GFP derivatives on nickel chelating beads
    • Youvan, D. C., Silva, C. M., Bylina, E. J., Coleman, W. J., Dilworth, M. R., and Yang, M. M. (1997) Calibration of fluorescence resonance energy transfer in microscopy using genetically engineered GFP derivatives on nickel chelating beads. Biotechnol. Alia 3, 1-18
    • (1997) Biotechnol. Alia , vol.3 , pp. 1-18
    • Youvan, D.C.1    Silva, C.M.2    Bylina, E.J.3    Coleman, W.J.4    Dilworth, M.R.5    Yang, M.M.6
  • 18
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • DOI 10.1016/j.copbio.2004.12.002, PII S0958166904001673
    • Wallrabe, H., and Periasamy, A. (2005) Imaging protein molecules using FRET and FLIM microscopy. Curr. Opin. Biotechnol. 16, 19-27 (Pubitemid 40249755)
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.1 SPEC. ISSUE , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 19
    • 0001406574 scopus 로고
    • Guanylate cyclase. GT Ppyrophosphatelyase (cyclizing) EC 4.6.1.2
    • Bergmeyer, H. U., Bergmeyer, J., and Grassl, M., eds., 3rd Ed., Verlag Chemie, Weihheim, Germany
    • Schultz, G., and Böhme, E. (1984) Guanylate cyclase. GT Ppyrophosphatelyase (cyclizing) EC 4.6.1.2 in Method of Enzymatic Analysis (Bergmeyer, H. U., Bergmeyer, J., and Grassl, M., eds.), 3rd Ed., Verlag Chemie, pp 379-389, Weihheim, Germany
    • (1984) Method of Enzymatic Analysis , pp. 379-389
    • Schultz, G.1    Böhme, E.2
  • 22
    • 33846491964 scopus 로고    scopus 로고
    • NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism
    • DOI 10.1038/sj.emboj.7601521, PII 7601521
    • Ma, X., Sayed, N., Beuve, A., and Van Den Akker, F. (2007) NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism. EMBO J. 26, 578-588 (Pubitemid 46160957)
    • (2007) EMBO Journal , vol.26 , Issue.2 , pp. 578-588
    • Ma, X.1    Sayed, N.2    Beuve, A.3    Van Den Akker, F.4
  • 24
    • 77649085537 scopus 로고    scopus 로고
    • Crystal structure of the signaling helix coiled-coil domain of the β-1 subunit of the soluble guanylyl cyclase
    • Ma, X., Beuve, A., and Van Den Akker, F. (2010) Crystal structure of the signaling helix coiled-coil domain of the β-1 subunit of the soluble guanylyl cyclase. BMC Struct. Biol. 10, 2
    • (2010) BMC Struct. Biol. , vol.10 , pp. 2
    • Ma, X.1    Beuve, A.2    Van Den Akker, F.3
  • 25
    • 34248371291 scopus 로고    scopus 로고
    • The signaling helix: A common functional theme in diverse signaling proteins
    • DOI 10.1186/1745-6150-1-25
    • Anantharaman, V., Balaji, S., and Aravind, L. (2006) The signaling helix: a common functional theme in diverse signaling proteins. Biol. Direct 1, 10. 1186/1745-6150-1-25 (Pubitemid 46730975)
    • (2006) Biology Direct , vol.1 , pp. 25
    • Anantharaman, V.1    Balaji, S.2    Aravind, L.3
  • 27
    • 84876841559 scopus 로고    scopus 로고
    • Higherorder interactions bridge the nitric oxide receptor and catalytic domains of soluble guanylate cyclase
    • Underbakke, E. S., Iavarone, A. T., and Marletta, M. A. (2013) Higherorder interactions bridge the nitric oxide receptor and catalytic domains of soluble guanylate cyclase. Proc. Natl. Acad. Sci. U. S. A. 110, 6777-6782
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 6777-6782
    • Underbakke, E.S.1    Iavarone, A.T.2    Marletta, M.A.3
  • 28
    • 0037809223 scopus 로고    scopus 로고
    • 1 subunit of soluble guanylyl cyclase is necessary for activation of the enzyme by nitric oxide and YC-1 but is not involved in heme binding
    • DOI 10.1074/jbc.M212740200
    • Koglin, M., and Behrends, S. (2003) A functional domain of the alpha1 subunit of soluble guanylyl cyclase is necessary for activation of the enzyme by nitric oxide and YC-1 but is not involved in heme binding. J. Biol. Chem. 278, 12590-12597 (Pubitemid 36800249)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 12590-12597
    • Koglin, M.1    Behrends, S.2
  • 29
    • 84871576386 scopus 로고    scopus 로고
    • Picosecond to second dynamics reveals a structural transition in clostridium botulinum NO-sensor triggered by the activator BAY-41-2272
    • Yoo, B. K., Lamarre, I., Rappaport, F., Nioche, P., Raman, C. S., Martin, J. L., and Negrerie, M. (2012) Picosecond to Second Dynamics Reveals a Structural Transition in Clostridium botulinum NO-Sensor Triggered by the Activator BAY-41-2272. ACS Chem. Biol. 7, 2046-2054
    • (2012) ACS Chem. Biol. , vol.7 , pp. 2046-2054
    • Yoo, B.K.1    Lamarre, I.2    Rappaport, F.3    Nioche, P.4    Raman, C.S.5    Martin, J.L.6    Negrerie, M.7
  • 30
    • 84891692457 scopus 로고    scopus 로고
    • Crystal structure of the Alpha subunit PAS domain from soluble guanylyl cyclase
    • Purohit, R., Weichsel, A., and Montfort, W. R. (2013) Crystal structure of the Alpha subunit PAS domain from soluble guanylyl cyclase. Protein Sci. 22, 1439-1444
    • (2013) Protein Sci. , vol.22 , pp. 1439-1444
    • Purohit, R.1    Weichsel, A.2    Montfort, W.R.3
  • 31
    • 10044276844 scopus 로고    scopus 로고
    • NO activation of guanylyl cyclase
    • DOI 10.1038/sj.emboj.7600422
    • Russwurm, M., and Koesling, D. (2004) NO activation of guanylyl cyclase. EMBO J. 23, 4443-4450 (Pubitemid 39601969)
    • (2004) EMBO Journal , vol.23 , Issue.22 , pp. 4443-4450
    • Russwurm, M.1    Koesling, D.2
  • 32
    • 77954568592 scopus 로고    scopus 로고
    • Structure of cinaciguat (bay 58-2667) bound to nostoc H-NOX domain reveals insights into heme-mimetic activation of the soluble guanylyl cyclase
    • Martin, F., Baskaran, P., Ma, X., Dunten, P. W., Schaefer, M., Stasch, J. P., Beuve, A., and Van Den Akker, F. (2010) Structure of cinaciguat (bay 58-2667) bound to nostoc H-NOX domain reveals insights into heme-mimetic activation of the soluble guanylyl cyclase. J. Biol. Chem. 285, 22651-22657
    • (2010) J. Biol. Chem. , vol.285 , pp. 22651-22657
    • Martin, F.1    Baskaran, P.2    Ma, X.3    Dunten, P.W.4    Schaefer, M.5    Stasch, J.P.6    Beuve, A.7    Van Den Akker, F.8
  • 33
    • 38149078912 scopus 로고    scopus 로고
    • PAS-mediated dimerization of soluble guanylyl cyclase revealed by signal transduction histidine kinase domain crystal structure
    • Ma, X., Sayed, N., Baskaran, P., Beuve, A., and Van Den Akker, F. (2008) PAS-mediated dimerization of soluble guanylyl cyclase revealed by signal transduction histidine kinase domain crystal structure. J. Biol. Chem. 283, 1167-1178
    • (2008) J. Biol. Chem. , vol.283 , pp. 1167-1178
    • Ma, X.1    Sayed, N.2    Baskaran, P.3    Beuve, A.4    Van Den Akker, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.