메뉴 건너뛰기




Volumn 17, Issue 9, 2012, Pages 1178-1189

Unusual heme binding properties of the dissimilative nitrate respiration regulator, a bacterial nitric oxide sensor

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP RECEPTOR; DISSIMILATIVE NITRATE RESPIRATION REGULATOR; FUMARIC ACID; HEME; HEMOPROTEIN; HISTIDINE; NITRATE REDUCTASE; NITRIC OXIDE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 84865627725     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2011.4226     Document Type: Article
Times cited : (23)

References (52)
  • 1
    • 0029146375 scopus 로고
    • Expression of the nir and nor genes for denitrification of Pseudomonas aeruginosa requires a novel CRP/FNR-related transcriptional regulator, DNR, in addition to ANR
    • Arai H, Igarashi Y, and Kodama T. Expression of the nir and nor genes for denitrification of Pseudomonas aeruginosa requires a novel CRP/FNR-related transcriptional regulator, DNR, in addition to ANR. FEBS Lett 371:73-76, 1995.
    • (1995) FEBS Lett , vol.371 , pp. 73-76
    • Arai, H.1    Igarashi, Y.2    Kodama, T.3
  • 5
    • 69949151824 scopus 로고    scopus 로고
    • The transcription factor DNR from Pseudomonas aeruginosa specifically requires nitric oxide and haem for the activation of a target promoter in Escherichia coli
    • Castiglione N, Rinaldo S, Giardina G, and Cutruzzolà F. The transcription factor DNR from Pseudomonas aeruginosa specifically requires nitric oxide and haem for the activation of a target promoter in Escherichia coli. Microbiology 155:2838-2844, 2009.
    • (2009) Microbiology , vol.155 , pp. 2838-2844
    • Castiglione, N.1    Rinaldo, S.2    Giardina, G.3    Cutruzzolà, F.4
  • 6
    • 33751337777 scopus 로고    scopus 로고
    • Insight into heme protein redox potential control and functional aspects of six-coordinate ligand-sensing heme proteins from studies of synthetic heme peptides
    • Cowley AB, Kennedy ML, Silchenko S, Lukat-Rodgers GS, Rodgers KR, and Benson DR. Insight into heme protein redox potential control and functional aspects of six-coordinate ligand-sensing heme proteins from studies of synthetic heme peptides. Inorg Chem 45:9985-10001, 2006.
    • (2006) Inorg Chem , vol.45 , pp. 9985-10001
    • Cowley, A.B.1    Kennedy, M.L.2    Silchenko, S.3    Lukat-Rodgers, G.S.4    Rodgers, K.R.5    Benson, D.R.6
  • 9
    • 77957325735 scopus 로고    scopus 로고
    • Reconstruction of the core and extended regulons of global transcription factors
    • Dufour YS, Kiley PJ, and Donohue TJ. Reconstruction of the core and extended regulons of global transcription factors. PLoS Genet 6:e1001027, 2010.
    • (2010) PLoS Genet , vol.6
    • Dufour, Y.S.1    Kiley, P.J.2    Donohue, T.J.3
  • 10
    • 17144398027 scopus 로고    scopus 로고
    • The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif
    • DOI 10.1111/j.1365-2958.2005.04561.x
    • Eiting M, Hagelüken G, Schubert WD, and Heinz DW. The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif. Mol Microbiol 56:433-446, 2005. (Pubitemid 40516782)
    • (2005) Molecular Microbiology , vol.56 , Issue.2 , pp. 433-446
    • Eiting, M.1    Hageluken, G.2    Schubert, W.-D.3    Heinz, D.W.4
  • 11
    • 67649745795 scopus 로고    scopus 로고
    • Profound asymmetry in the structure of the cAMP-free cAMP Receptor Protein (CRP) from Mycobacterium tuberculosis
    • Gallagher D, Smith N, Kim S, Robinson H, and Reddy P. Profound asymmetry in the structure of the cAMP-free cAMP Receptor Protein (CRP) from Mycobacterium tuberculosis. J Biol Chem 284:8228-8232, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 8228-8232
    • Gallagher, D.1    Smith, N.2    Kim, S.3    Robinson, H.4    Reddy, P.5
  • 12
    • 70349334424 scopus 로고    scopus 로고
    • A dramatic conformational rearrangement is necessary for the activation of DNR from Pseudomonas aeruginosa. Crystal structure of wild-type DNR
    • Giardina G, Rinaldo S, Castiglione N, Caruso M, and Cutruzzolà F. A dramatic conformational rearrangement is necessary for the activation of DNR from Pseudomonas aeruginosa. Crystal structure of wild-type DNR. Proteins 77:174-180, 2009.
    • (2009) Proteins , vol.77 , pp. 174-180
    • Giardina, G.1    Rinaldo, S.2    Castiglione, N.3    Caruso, M.4    Cutruzzolà, F.5
  • 14
    • 0023042546 scopus 로고
    • A kinetic description of ligand binding to sperm whale myoglobin
    • Gibson QH, Olson JS, McKinnie RE, and Rohlfs RJ. A kinetic description of ligand binding to sperm whale myoglobin. J Biol Chem 261:10228-10239, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 10228-10239
    • Gibson, Q.H.1    Olson, J.S.2    McKinnie, R.E.3    Rohlfs, R.J.4
  • 15
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses
    • DOI 10.1016/j.jinorgbio.2004.11.006, PII S0162013404003502, Heme-Diatomic Interactions, Part 1
    • Gilles-Gonzalez MA and Gonzalez G. Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses. J Inorg Biochem 99:1-22, 2005. (Pubitemid 39642968)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 1-22
    • Gilles-Gonzalez, M.-A.1    Gonzalez, G.2
  • 16
    • 70350457954 scopus 로고    scopus 로고
    • Cyclic-di-GMP-binding CRP-like protein: A spectacular new role for a veteran signal transduction actor
    • Gomelsky M. Cyclic-di-GMP-binding CRP-like protein: A spectacular new role for a veteran signal transduction actor. J Bacteriol 191:6785-6787, 2009.
    • (2009) J Bacteriol , vol.191 , pp. 6785-6787
    • Gomelsky, M.1
  • 17
    • 0034982114 scopus 로고    scopus 로고
    • Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP
    • DOI 10.1016/S0065-2911(01)44010-0
    • Green J, Scott C, and Guest JR. Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP. Adv Microb Physiol 44:1-34, 2001. (Pubitemid 32500109)
    • (2001) Advances in Microbial Physiology , vol.44 , pp. 1-34
    • Green, J.1    Scott, C.2    Guest, J.R.3
  • 19
    • 79251600033 scopus 로고    scopus 로고
    • Hemebinding characteristics of the isolated PAS-B domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms
    • Hayasaka K, Kitanishi K, Igarashi J, and Shimizu T. Hemebinding characteristics of the isolated PAS-B domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms. Biochim Biophys Acta 1814:326-333, 2011.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 326-333
    • Hayasaka, K.1    Kitanishi, K.2    Igarashi, J.3    Shimizu, T.4
  • 20
    • 0015223110 scopus 로고
    • Origin of the heme Cotton effects in myoglobin and hemoglobin
    • Hsu MC and Wood RW. Origin of the heme Cotton effects in myoglobin and hemoglobin. J Am Chem Soc 93:3515-3525, 1971.
    • (1971) J Am Chem Soc , vol.93 , pp. 3515-3525
    • Hsu, M.C.1    Wood, R.W.2
  • 21
    • 49649105752 scopus 로고    scopus 로고
    • Elucidation of the heme binding site of heme-regulated eukaryotic initiation factor 2alpha kinase and the role of the regulatory motif in heme sensing by spectroscopic and catalytic studies of mutant proteins
    • Igarashi J, Murase M, Iizuka A, Pichierri F, Martinkova M, and Shimizu T. Elucidation of the heme binding site of heme-regulated eukaryotic initiation factor 2alpha kinase and the role of the regulatory motif in heme sensing by spectroscopic and catalytic studies of mutant proteins. J Biol Chem 283:18782-18791, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 18782-18791
    • Igarashi, J.1    Murase, M.2    Iizuka, A.3    Pichierri, F.4    Martinkova, M.5    Shimizu, T.6
  • 23
    • 50149095403 scopus 로고    scopus 로고
    • Arg97 at the heme-distal side of the isolated hemebound PAS domain of a heme-based oxygen sensor from Escherichia coli (Ec DOS) plays critical roles in autoxidation and binding to gases, particularly O2
    • Ishitsuka Y, Araki Y, Tanaka A, Igarashi J, Ito O, and Shimizu T. Arg97 at the heme-distal side of the isolated hemebound PAS domain of a heme-based oxygen sensor from Escherichia coli (Ec DOS) plays critical roles in autoxidation and binding to gases, particularly O2. Biochemistry 47:8874-8884, 2008.
    • (2008) Biochemistry , vol.47 , pp. 8874-8884
    • Ishitsuka, Y.1    Araki, Y.2    Tanaka, A.3    Igarashi, J.4    Ito, O.5    Shimizu, T.6
  • 25
    • 0031006612 scopus 로고    scopus 로고
    • Kinetics of nitric oxide dissociation from five- and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase
    • DOI 10.1021/bi970201o
    • Kharitonov VG, Sharma VS, Magde D, and Koesling D. Kinetics of nitric oxide dissociation from five-and six-coordinate nitrosyl hemes and heme proteins, including soluble guanylate cyclase. Biochemistry 36:6814-6818, 1997. (Pubitemid 27242342)
    • (1997) Biochemistry , vol.36 , Issue.22 , pp. 6814-6818
    • Kharitonov, V.G.1    Sharma, V.S.2    Magde, D.3    Koesling, D.4
  • 26
    • 44949200347 scopus 로고    scopus 로고
    • Heme-binding characteristics of the isolated PAS-A domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms
    • DOI 10.1021/bi7023892
    • Kitanishi K, Igarashi J, Hayasaka K, Hikage N, Saiful I, Yamauchi S, Uchida T, Ishimori K, and Shimizu T. Hemebinding characteristics of the isolated PAS-A domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms. Biochemistry 47:6157-6168, 2008. (Pubitemid 351812828)
    • (2008) Biochemistry , vol.47 , Issue.23 , pp. 6157-6168
    • Kitanishi, K.1    Igarashi, J.2    Hayasaka, K.3    Hikage, N.4    Saiful, I.5    Yamauchi, S.6    Uchida, T.7    Ishimori, K.8    Shimizu, T.9
  • 27
    • 0344153756 scopus 로고    scopus 로고
    • Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: Exploiting the metabolic spectrum by controlling alternative gene programs
    • DOI 10.1016/S0168-6445(03)00066-4
    • Körner H, Sofia HJ, and Zumft WG. Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs. FEMS Microbiol Rev 27:559-592, 2003. (Pubitemid 37456858)
    • (2003) FEMS Microbiology Reviews , vol.27 , Issue.5 , pp. 559-592
    • Korner, H.1    Sofia, H.J.2    Zumft, W.G.3
  • 29
    • 67650458070 scopus 로고    scopus 로고
    • Guanidine hydrochloride-induced unfolding of the three heme coordination states of the CO-sensing transcription factor, CooA
    • Lee AJ, Clark RW, Youn H, Ponter S, and Burstyn JN. Guanidine hydrochloride-induced unfolding of the three heme coordination states of the CO-sensing transcription factor, CooA. Biochemistry 48:6585-6597, 2009.
    • (2009) Biochemistry , vol.48 , pp. 6585-6597
    • Lee, A.J.1    Clark, R.W.2    Youn, H.3    Ponter, S.4    Burstyn, J.N.5
  • 30
    • 33646765404 scopus 로고    scopus 로고
    • * alleles encoding effectorindependent proteins and evidence for a haem-based sensing mechanism
    • * alleles encoding effectorindependent proteins and evidence for a haem-based sensing mechanism. Microbiology 152:1461-1470, 2006.
    • (2006) Microbiology , vol.152 , pp. 1461-1470
    • Lee, Y.Y.1    Shearer, N.2    Spiro, S.3
  • 32
    • 0032078948 scopus 로고    scopus 로고
    • Transcription activation by Escherichia coli FNR protein: Similarities to, and differences from, the CRP paradigm
    • DOI 10.1093/nar/26.9.2075
    • Li B, Wing H, Lee D, Wu H, and Busby S. Transcription activation by Escherichia coli FNR protein: similarities to, and differences from, the CRP paradigm. Nucleic Acids Res 26:2075-2081, 1998. (Pubitemid 28291748)
    • (1998) Nucleic Acids Research , vol.26 , Issue.9 , pp. 2075-2081
    • Li, B.1    Wing, H.2    Lee, D.3    Wu, H.-C.4    Busby, S.5
  • 33
    • 79952107782 scopus 로고    scopus 로고
    • Structural analysis of heme proteins: Implications for design and prediction
    • Li T, Bonkovsky H, and Guo J. Structural analysis of heme proteins: implications for design and prediction. BMC Struct Biol 11-13, 2011.
    • (2011) BMC Struct Biol , pp. 11-13
    • Li, T.1    Bonkovsky, H.2    Guo, J.3
  • 34
    • 0028773015 scopus 로고
    • Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • Martinez SE, Huang D, Szczepaniak A, Cramer WA, and Smith JL. Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. Structure 2:95-105, 1994. (Pubitemid 124002012)
    • (1994) Structure , vol.2 , Issue.2 , pp. 95-105
    • Martinez, S.E.1    Huang, D.2    Szczepaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 35
    • 0019463941 scopus 로고
    • Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA
    • DOI 10.1038/290744a0
    • McKay DB and Steitz TA. Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to lefthanded B-DNA. Nature 290:744-749, 1981. (Pubitemid 11068041)
    • (1981) Nature , vol.290 , Issue.5809 , pp. 744-749
    • McKay, D.B.1    Steitz, T.A.2
  • 36
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller JH. Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1972, pp. 352-355.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 40
    • 79952812426 scopus 로고    scopus 로고
    • Unusual heme-binding PAS domain from YybT family proteins
    • Rao F, Ji Q, Soehano I, and Liang Z. Unusual heme-binding PAS domain from YybT family proteins. J Bacteriol 193:1543-1551, 2011.
    • (2011) J Bacteriol , vol.193 , pp. 1543-1551
    • Rao, F.1    Ji, Q.2    Soehano, I.3    Liang, Z.4
  • 41
    • 14644401763 scopus 로고    scopus 로고
    • N-oxide sensing in Pseudomonas aeruginosa: Expression and preliminary characterization of DNR, an FNR-CRP type transcriptional regulator
    • DOI 10.1042/BST0330184
    • Rinaldo S, Giardina G, Brunori M, and Cutruzzola F. N-oxide sensing in Pseudomonas aeruginosa: expression and preliminary characterization of DNR, an FNR-CRP type transcriptional regulator. Biochem Soc Trans 33:184-186, 2005. (Pubitemid 40313796)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.1 , pp. 184-186
    • Rinaldo, S.1    Giardina, G.2    Brunori, M.3    Cutruzzola, F.4
  • 42
    • 10444220187 scopus 로고    scopus 로고
    • CooA, a paradigm for gas sensing regulatory proteins
    • DOI 10.1016/j.jinorgbio.2004.10.032, PII S0162013404003393, Heme-Diatomic Interactions, Part 1
    • Roberts GP, Kerby RL, Youn H, and Conrad M. CooA, a paradigm for gas sensing regulatory proteins. J Inorg Biochem 99:280-292, 2005. (Pubitemid 39642982)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 280-292
    • Roberts, G.P.1    Kerby, R.L.2    Youn, H.3    Conrad, M.4
  • 43
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • Savitzky A and Golay M J E. Smoothing and Differentiation of Data by Simplified Least Squares Procedures. Anal Chem 36:1627-1639, 1964.
    • (1964) Anal Chem , vol.36 , pp. 1627-1639
    • Savitzky, A.1    Golay, M.J.E.2
  • 44
    • 30744469606 scopus 로고    scopus 로고
    • Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species
    • DOI 10.1021/bi051902l
    • Smagghe BJ, Sarath G, Ross E, Hilbert JL, and Hargrove MS. Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species. Biochemistry 45:561-570, 2006. (Pubitemid 43100421)
    • (2006) Biochemistry , vol.45 , Issue.2 , pp. 561-570
    • Smagghe, B.J.1    Sarath, G.2    Ross, E.3    Hilbert, J.-L.4    Hargrove, M.S.5
  • 45
    • 75749117906 scopus 로고    scopus 로고
    • The cyclic nucleotide monophosphate domain of Xanthomonas campestris global regulator Clp defines a new class of cyclic di-GMP effectors
    • Tao F, He YW, Wu DH, Swarup S, and Zhang LH. The cyclic nucleotide monophosphate domain of Xanthomonas campestris global regulator Clp defines a new class of cyclic di-GMP effectors. J Bacteriol 192:1020-1029, 2010.
    • (2010) J Bacteriol , vol.192 , pp. 1020-1029
    • Tao, F.1    He, Y.W.2    Wu, D.H.3    Swarup, S.4    Zhang, L.H.5
  • 46
    • 70450191983 scopus 로고    scopus 로고
    • Dynamic activation of an allosteric regulatory protein
    • Tzeng SR and Kalodimos CG. Dynamic activation of an allosteric regulatory protein. Nature 462:368-372, 2009.
    • (2009) Nature , vol.462 , pp. 368-372
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 47
    • 34547631100 scopus 로고    scopus 로고
    • Nitrate sensing and metabolism modulate motility, biofilm formation, and virulence in Pseudomonas aeruginosa
    • DOI 10.1128/IAI.00201-07
    • Van Alst NE, Picardo KF, Iglewski BH, and Haidaris CG. Nitrate sensing and metabolism modulate motility, biofilm formation, and virulence in Pseudomonas aeruginosa. Infect Immun 75:3780-3790, 2007. (Pubitemid 47206275)
    • (2007) Infection and Immunity , vol.75 , Issue.8 , pp. 3780-3790
    • Van Alst, N.E.1    Picardo, K.F.2    Iglewski, B.H.3    Haidaris, C.G.4
  • 48
    • 0035091010 scopus 로고    scopus 로고
    • Nitric oxide signaling and transcriptional control of denitrification genes in Pseudomonas stutzeri
    • DOI 10.1128/JB.183.8.2516-2526.2001
    • Vollack KU and Zumft WG. Nitric oxide signaling and transcriptional control of denitrification genes in Pseudomonas stutzeri. J Bacteriol 183:2516-2526, 2001. (Pubitemid 32249760)
    • (2001) Journal of Bacteriology , vol.183 , Issue.8 , pp. 2516-2526
    • Vollack, K.-U.1    Zumft, W.G.2
  • 49
    • 69249241732 scopus 로고    scopus 로고
    • Structural overview on the allosteric activation of cyclic AMP receptor protein
    • Won H, Lee Y, Lee S, and Lee B. Structural overview on the allosteric activation of cyclic AMP receptor protein. Biochim Biophys Acta 1794:1299-1308, 2009.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 1299-1308
    • Won, H.1    Lee, Y.2    Lee, S.3    Lee, B.4
  • 50
    • 14844355242 scopus 로고    scopus 로고
    • Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein
    • DOI 10.1074/jbc.M411664200
    • Yang J, Ishimori K, and O'Brian MR. Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein. J Biol Chem 280:7671-7676, 2005. (Pubitemid 40352575)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 7671-7676
    • Yang, J.1    Ishimori, K.2    O'Brian, M.R.3
  • 51
    • 76149085834 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy
    • Yano J and Yachandra VK. X-ray absorption spectroscopy. Photosynth Res 102:241-254, 2009.
    • (2009) Photosynth Res , vol.102 , pp. 241-254
    • Yano, J.1    Yachandra, V.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.