메뉴 건너뛰기




Volumn 46, Issue 50, 2007, Pages 14629-14637

Measurement of the heme affinity for yeast Dap1p, and its importance in cellular function

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL FUNCTIONING; CELLULAR FUNCTIONS; ERGOSTEROL BIOSYNTHESIS; HEME AFFINITY;

EID: 37249017475     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7013739     Document Type: Article
Times cited : (26)

References (40)
  • 1
    • 0029900104 scopus 로고    scopus 로고
    • Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes
    • Meyer, C., Schmid, R., Scriba, P. C., and Wehling, M. (1996) Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes, Eur. J. Biochem. 239, 726-731.
    • (1996) Eur. J. Biochem , vol.239 , pp. 726-731
    • Meyer, C.1    Schmid, R.2    Scriba, P.C.3    Wehling, M.4
  • 2
    • 0030569560 scopus 로고    scopus 로고
    • Full-length cDNA sequence of a progesterone membrane-binding protein from porcine vascular smooth muscle cells
    • Falkenstein, E., Meyer, C., Eisen, C., Scriba, P. C., and Wehling, M. (1996) Full-length cDNA sequence of a progesterone membrane-binding protein from porcine vascular smooth muscle cells, Biochem. Biophys. Res. Commun. 229, 86-89.
    • (1996) Biochem. Biophys. Res. Commun , vol.229 , pp. 86-89
    • Falkenstein, E.1    Meyer, C.2    Eisen, C.3    Scriba, P.C.4    Wehling, M.5
  • 3
    • 0035068387 scopus 로고    scopus 로고
    • Chemical modification and structural analysis of the progesterone membrane binding protein from porcine liver membranes
    • Falkenstein, E., Eisen, C., Schmieding, K., Krautkramer, M., Stein, C., Losel, R., and Wehling, M. (2001) Chemical modification and structural analysis of the progesterone membrane binding protein from porcine liver membranes, Mol. Cell. Biochem. 218, 71-79.
    • (2001) Mol. Cell. Biochem , vol.218 , pp. 71-79
    • Falkenstein, E.1    Eisen, C.2    Schmieding, K.3    Krautkramer, M.4    Stein, C.5    Losel, R.6    Wehling, M.7
  • 8
    • 14044252188 scopus 로고    scopus 로고
    • Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae
    • Mallory, J. C., Crudden, G., Johnson, B. L., Mo, C., Pierson, C. A., Bard, M., and Craven, R. J. (2005) Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae, Mol. Cell. Biol. 25, 1669-1679.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 1669-1679
    • Mallory, J.C.1    Crudden, G.2    Johnson, B.L.3    Mo, C.4    Pierson, C.A.5    Bard, M.6    Craven, R.J.7
  • 11
    • 0038397236 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Dap1p, a novel DNA damage response protein related to the mammalian membrane-associated progesterone receptor
    • Hand, R. A., Jia, N., Bard, M., and Craven, R. J. (2003) Saccharomyces cerevisiae Dap1p, a novel DNA damage response protein related to the mammalian membrane-associated progesterone receptor, Eukaryotic Cell 2, 306-317.
    • (2003) Eukaryotic Cell , vol.2 , pp. 306-317
    • Hand, R.A.1    Jia, N.2    Bard, M.3    Craven, R.J.4
  • 12
    • 0029994433 scopus 로고    scopus 로고
    • Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis
    • Ooi, C. E., Rabinovich, E., Dancis, A., Bonifacino, J. S., and Klausner, R. D. (1996) Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis, EMBO J. 15, 3515-3523.
    • (1996) EMBO J , vol.15 , pp. 3515-3523
    • Ooi, C.E.1    Rabinovich, E.2    Dancis, A.3    Bonifacino, J.S.4    Klausner, R.D.5
  • 14
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A., and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra, Anal. Biochem. 161, 1-15.
    • (1987) Anal. Biochem , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 15
    • 0027976593 scopus 로고
    • Deconvolutions based on singular value decomposition and the pseudoinverse: A guide for beginners
    • Hendler, R. W., and Shrager, R. I. (1994) Deconvolutions based on singular value decomposition and the pseudoinverse: a guide for beginners, J. Biochem. Biophys. Methods 28, 1-33.
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 1-33
    • Hendler, R.W.1    Shrager, R.I.2
  • 16
    • 0029737827 scopus 로고    scopus 로고
    • The stability of holomyoglobin is determined by heme affinity
    • Hargrove, M. S., and Olson, J. S. (1996) The stability of holomyoglobin is determined by heme affinity, Biochemistry 35, 11310-11318.
    • (1996) Biochemistry , vol.35 , pp. 11310-11318
    • Hargrove, M.S.1    Olson, J.S.2
  • 17
    • 0029737668 scopus 로고    scopus 로고
    • Structural factors governing hemin dissociation from metmyoglobin
    • Hargrove, M. S., Wilkinson, A. J., and Olson, J. S. (1996) Structural factors governing hemin dissociation from metmyoglobin, Biochemistry 35, 11300-11309.
    • (1996) Biochemistry , vol.35 , pp. 11300-11309
    • Hargrove, M.S.1    Wilkinson, A.J.2    Olson, J.S.3
  • 18
    • 33846099581 scopus 로고    scopus 로고
    • Thermodynamic investigation into the mechanisms of proton-coupled electron transfer events in heme protein maquettes
    • Reddi, A. R., Reedy, C. J., Mui, S., and Gibney, B. R. (2007) Thermodynamic investigation into the mechanisms of proton-coupled electron transfer events in heme protein maquettes, Biochemistry 46, 291-305.
    • (2007) Biochemistry , vol.46 , pp. 291-305
    • Reddi, A.R.1    Reedy, C.J.2    Mui, S.3    Gibney, B.R.4
  • 19
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton, P. L. (1978) Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems, Methods Enzymol. 54, 411-435.
    • (1978) Methods Enzymol , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 20
    • 29244483674 scopus 로고    scopus 로고
    • Hpr6 (heme-1 domain protein) regulates the susceptibility of cancer cells to chemotherapeutic drugs
    • Crudden, G., Chitti, R. E., and Craven, R. J. (2005) Hpr6 (heme-1 domain protein) regulates the susceptibility of cancer cells to chemotherapeutic drugs, J. Pharmacol. Exp. Ther. 316, 448-455.
    • (2005) J. Pharmacol. Exp. Ther , vol.316 , pp. 448-455
    • Crudden, G.1    Chitti, R.E.2    Craven, R.J.3
  • 22
    • 37249050205 scopus 로고
    • Acetone extraction of heme from myoglobin and hemoglobin at acid pH
    • Fronticelli, C., and Bucci, E. (1963) Acetone extraction of heme from myoglobin and hemoglobin at acid pH, Biochim. Biophys. Acta 78, 530-531.
    • (1963) Biochim. Biophys. Acta , vol.78 , pp. 530-531
    • Fronticelli, C.1    Bucci, E.2
  • 23
    • 49749199032 scopus 로고
    • Cleavage of the haem-protein link by acid methylethylketone
    • Teale, F. W. J. (1959) Cleavage of the haem-protein link by acid methylethylketone, Biochim. Biophys. Acta 35, 543.
    • (1959) Biochim. Biophys. Acta , vol.35 , pp. 543
    • Teale, F.W.J.1
  • 24
    • 0037424025 scopus 로고    scopus 로고
    • Thermodynamic characterization of ferric and ferrous haem binding to a designed four-alpha-helix protein
    • Reedy, C. J., Kennedy, M. L., and Gibney, B. R. (2003) Thermodynamic characterization of ferric and ferrous haem binding to a designed four-alpha-helix protein, Chem. Commun. (Cambridge, U.K.), 570-571.
    • (2003) Chem. Commun. (Cambridge, U.K.) , pp. 570-571
    • Reedy, C.J.1    Kennedy, M.L.2    Gibney, B.R.3
  • 25
    • 4544231687 scopus 로고    scopus 로고
    • Direct electrochemistry of catalase at a gold electrode modified with single-wall carbon nanotubes
    • Wang, L., Wang, J., and Zhou, F. (2004) Direct electrochemistry of catalase at a gold electrode modified with single-wall carbon nanotubes, Electroanalysis 16, 627-632.
    • (2004) Electroanalysis , vol.16 , pp. 627-632
    • Wang, L.1    Wang, J.2    Zhou, F.3
  • 27
    • 1542274547 scopus 로고    scopus 로고
    • Heme protein assemblies
    • Reedy, C. J., and Gibney, B. R. (2004) Heme protein assemblies, Chem. Rev. 104, 617-649.
    • (2004) Chem. Rev , vol.104 , pp. 617-649
    • Reedy, C.J.1    Gibney, B.R.2
  • 28
    • 34547422800 scopus 로고    scopus 로고
    • Cloning and characterization of a novel periplasmic heme-transport protein from the human pathogen Pseudomonas aeruginosa
    • Tong, Y., and Guo, M. (2007) Cloning and characterization of a novel periplasmic heme-transport protein from the human pathogen Pseudomonas aeruginosa, J. Biol. Inorg. Chem. 12, 735-750.
    • (2007) J. Biol. Inorg. Chem , vol.12 , pp. 735-750
    • Tong, Y.1    Guo, M.2
  • 29
    • 0029737895 scopus 로고    scopus 로고
    • The association rate constant for heme binding to globin is independent of protein structure
    • Hargrove, M. S., Barrick, D., and Olson, J. S. (1996) The association rate constant for heme binding to globin is independent of protein structure, Biochemistry 35, 11293-11299.
    • (1996) Biochemistry , vol.35 , pp. 11293-11299
    • Hargrove, M.S.1    Barrick, D.2    Olson, J.S.3
  • 30
    • 0345114077 scopus 로고
    • Hard and soft acids and bases
    • Pearson, R. G. (1963) Hard and soft acids and bases, J. Am. Chem. Soc. 85, 3533-3539.
    • (1963) J. Am. Chem. Soc , vol.85 , pp. 3533-3539
    • Pearson, R.G.1
  • 32
    • 1442328094 scopus 로고    scopus 로고
    • Electron tunneling through proteins
    • Gray, H. B., and Winkler, J. R. (2004) Electron tunneling through proteins, Q. Rev. Biophys. 36, 341-372.
    • (2004) Q. Rev. Biophys , vol.36 , pp. 341-372
    • Gray, H.B.1    Winkler, J.R.2
  • 33
    • 0027360859 scopus 로고
    • Sterol synthesis and viability of erg11 (cytochrome P450 lanosterol demethylase) mutations in Saccharomyces cerevisiae and Candida albicans
    • Bard, M., Lees, N. D., Turi, T., Craft, D., Cofrin, L., Barbuch, R., Koegel, C., and Loper, J. C. (1993) Sterol synthesis and viability of erg11 (cytochrome P450 lanosterol demethylase) mutations in Saccharomyces cerevisiae and Candida albicans, Lipids 28, 963-967.
    • (1993) Lipids , vol.28 , pp. 963-967
    • Bard, M.1    Lees, N.D.2    Turi, T.3    Craft, D.4    Cofrin, L.5    Barbuch, R.6    Koegel, C.7    Loper, J.C.8
  • 36
    • 0344393081 scopus 로고    scopus 로고
    • Effects of injury and progesterone treatment on progesterone receptor and progesterone binding protein 25-Dx expression in the rat spinal cord
    • Labombarda, F., Gonzalez, S. L., Deniselle, M. C., Vinson, G. P., Schumacher, M., De Nicola, A. F., and Guennoun, R. (2003) Effects of injury and progesterone treatment on progesterone receptor and progesterone binding protein 25-Dx expression in the rat spinal cord, J. Neurochem. 87, 902-913.
    • (2003) J. Neurochem , vol.87 , pp. 902-913
    • Labombarda, F.1    Gonzalez, S.L.2    Deniselle, M.C.3    Vinson, G.P.4    Schumacher, M.5    De Nicola, A.F.6    Guennoun, R.7
  • 37
    • 34247634992 scopus 로고    scopus 로고
    • Non-genomic actions of progesterone in the normal and neoplastic mammalian ovary
    • Peluso, J. J. (2007) Non-genomic actions of progesterone in the normal and neoplastic mammalian ovary, Semin. Reprod. Med. 25, 198-207.
    • (2007) Semin. Reprod. Med , vol.25 , pp. 198-207
    • Peluso, J.J.1
  • 38
    • 33646806787 scopus 로고    scopus 로고
    • Progesterone membrane receptor component 1 expression in the immature rat ovary and its role in mediating progesterone's antiapoptotic action
    • Peluso, J. J., Pappalardo, A., Losel, R., and Wehling, M. (2006) Progesterone membrane receptor component 1 expression in the immature rat ovary and its role in mediating progesterone's antiapoptotic action, Endocrinology 147, 3133-3140.
    • (2006) Endocrinology , vol.147 , pp. 3133-3140
    • Peluso, J.J.1    Pappalardo, A.2    Losel, R.3    Wehling, M.4
  • 40
    • 0033741196 scopus 로고    scopus 로고
    • A membrane-associated progesterone-binding protein, 25-Dx, is regulated by progesterone in brain regions involved in female reproductive behaviors
    • Krebs, C. J., Jarvis, E. D., Chan, J., Lydon, J. P., Ogawa, S., and Pfaff, D. W. (2000) A membrane-associated progesterone-binding protein, 25-Dx, is regulated by progesterone in brain regions involved in female reproductive behaviors, Proc. Natl. Acad. Sci. U.S.A. 97, 12816-12821.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 12816-12821
    • Krebs, C.J.1    Jarvis, E.D.2    Chan, J.3    Lydon, J.P.4    Ogawa, S.5    Pfaff, D.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.