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Volumn 272, Issue 16, 2005, Pages 4153-4162

Spectroscopic characterization of the isolated heme-bound PAS-B domain of neuronal PAS domain protein 2 associated with circadian rhythms

Author keywords

Circadian rhythms; Heme sensor protein; PAS domain; Resonance Raman spectroscopy; Transcription

Indexed keywords

ALANINE; HEMOPROTEIN; HISTIDINE; IRON COMPLEX; PROTEIN NPAS2; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 23844468462     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04828.x     Document Type: Article
Times cited : (30)

References (34)
  • 1
    • 0032510778 scopus 로고    scopus 로고
    • The basic-helix-loop-helix-PAS orphan MOPs forms transcriptionally active complexes with circadian and hypoxia factors
    • Hogenesch JB, Gu YZ, Jain S & Brandfield CA (1998) The basic-helix-loop-helix-PAS orphan MOPs forms transcriptionally active complexes with circadian and hypoxia factors. Proc Natl Acad Sci USA 95, 5474-5479.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5474-5479
    • Hogenesch, J.B.1    Gu, Y.Z.2    Jain, S.3    Brandfield, C.A.4
  • 2
    • 0035919479 scopus 로고    scopus 로고
    • Regulation of Clock and NPAS2 DNA Binding by the Redox State of NAD Cofactors
    • Rutter J, Reick M, Wu LC & McKnight SL (2001) Regulation of Clock and NPAS2 DNA Binding by the Redox State of NAD Cofactors. Science 293, 510-514.
    • (2001) Science , vol.293 , pp. 510-514
    • Rutter, J.1    Reick, M.2    Wu, L.C.3    McKnight, S.L.4
  • 3
    • 0037194790 scopus 로고    scopus 로고
    • Coordination of circadian timing in mammals
    • Reppert SM & Weaver DR (2002) Coordination of circadian timing in mammals. Nature 418, 935-941.
    • (2002) Nature , vol.418 , pp. 935-941
    • Reppert, S.M.1    Weaver, D.R.2
  • 4
    • 1342283142 scopus 로고    scopus 로고
    • Molecular mechanism of mammalian circadian clock
    • Isojima Y, Okumura N & Nagai K (2003) Molecular mechanism of mammalian circadian clock. J Biochem (Tokyo) 134, 777-784.
    • (2003) J Biochem (Tokyo) , vol.134 , pp. 777-784
    • Isojima, Y.1    Okumura, N.2    Nagai, K.3
  • 7
    • 0142244197 scopus 로고    scopus 로고
    • Liver regeneration clocks on
    • Schibler U (2003) Liver regeneration clocks on. Science 302, 234-235.
    • (2003) Science , vol.302 , pp. 234-235
    • Schibler, U.1
  • 9
    • 0042817947 scopus 로고    scopus 로고
    • Functional and structural analyses of cryptochrome: Vertebrate Cry regions responsible for interaction with the Clock:BMAL heterodimer and its nuclear locations
    • Hirayama J, Namura H, Ishikawa T, Kobayashi Y & Todo T (2003) Functional and structural analyses of cryptochrome: vertebrate Cry regions responsible for interaction with the Clock:BMAL heterodimer and its nuclear locations. J Biol Chem 278, 35620-35628.
    • (2003) J Biol Chem , vol.278 , pp. 35620-35628
    • Hirayama, J.1    Namura, H.2    Ishikawa, T.3    Kobayashi, Y.4    Todo, T.5
  • 10
    • 1942533607 scopus 로고    scopus 로고
    • Circadian lessons from peripheral clocks: Is the time of the mammalian pacemaker up?
    • Brandstaetter R (2004) Circadian lessons from peripheral clocks: is the time of the mammalian pacemaker up? Proc Natl Acad Sci USA 101, 5699-5700.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5699-5700
    • Brandstaetter, R.1
  • 11
    • 0035919618 scopus 로고    scopus 로고
    • NPAS2: An analog of Clock operative in the mammalian forebrain
    • Reick M, Garcia JA, Dudley C & McKnight SL (2001) NPAS2: an analog of Clock operative in the mammalian forebrain. Science 293, 506-509.
    • (2001) Science , vol.293 , pp. 506-509
    • Reick, M.1    Garcia, J.A.2    Dudley, C.3    McKnight, S.L.4
  • 13
    • 0035967914 scopus 로고    scopus 로고
    • Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: A humoral mechanism to reset a peripheral clock
    • McNamara P, Seo SP, Rudic RD, Sehgal A, Chakravarti D & FitzGerald GA (2001) Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: a humoral mechanism to reset a peripheral clock. Cell 105, 877-889.
    • (2001) Cell , vol.105 , pp. 877-889
    • McNamara, P.1    Seo, S.P.2    Rudic, R.D.3    Sehgal, A.4    Chakravarti, D.5    Fitzgerald, G.A.6
  • 15
    • 3343024625 scopus 로고    scopus 로고
    • Reciprocal regulation of haem biosynthesis and the circadian clock in mammals
    • Kaasik K & Lee CC (2004) Reciprocal regulation of haem biosynthesis and the circadian clock in mammals. Nature 430, 467-471.
    • (2004) Nature , vol.430 , pp. 467-471
    • Kaasik, K.1    Lee, C.C.2
  • 16
    • 0029819905 scopus 로고    scopus 로고
    • Determination of nitric oxide synthase cofactors: Heme, FAD, FMN, and tetrahydrobiopterin
    • Klatt P, Schmidt K, Werner ER & Mayer B (1996) Determination of nitric oxide synthase cofactors: heme, FAD, FMN, and tetrahydrobiopterin. Methods Enzymol 268, 358-365.
    • (1996) Methods Enzymol , vol.268 , pp. 358-365
    • Klatt, P.1    Schmidt, K.2    Werner, E.R.3    Mayer, B.4
  • 17
    • 0029737895 scopus 로고    scopus 로고
    • The association rate constant for heme binding to globin is independent of protein structure
    • Hargrove MS, Barrick D & Olson JS (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
  • 19
    • 0344807312 scopus 로고    scopus 로고
    • b-Type cytochrome electron carriers: Cytochromes 6562 and b5, and Flavocytochrome b2
    • (Messer-Schmidt A, Huber R, Poulos T & Wieghardt K, eds), John Wiley & Sons, Chichester
    • Mathews FS (2001) b-Type cytochrome electron carriers: cytochromes 6562 and b5, and Flavocytochrome b2. In Handbook of Metalloproteins (Messer-Schmidt A, Huber R, Poulos T & Wieghardt K, eds), vol. 1, pp. 159-171. John Wiley & Sons, Chichester.
    • (2001) Handbook of Metalloproteins , vol.1 , pp. 159-171
    • Mathews, F.S.1
  • 21
    • 8344236821 scopus 로고    scopus 로고
    • SOUL in mouse eye is a new hexameric heme-bound protein with characteristic optical absorption, resonance Raman spectral, and heme-binding properties
    • Sato E, Sagami I, Uchida T, Sato A, Kitagawa T, Igarashi J & Shimizu T (2004) SOUL in mouse eye is a new hexameric heme-bound protein with characteristic optical absorption, resonance Raman spectral, and heme-binding properties. Biochemistry 43, 14189-14198.
    • (2004) Biochemistry , vol.43 , pp. 14189-14198
    • Sato, E.1    Sagami, I.2    Uchida, T.3    Sato, A.4    Kitagawa, T.5    Igarashi, J.6    Shimizu, T.7
  • 22
    • 0037260847 scopus 로고    scopus 로고
    • Mechanisms of ligand discrimination by heme proteins
    • Jain R & Chan MK (2003) Mechanisms of ligand discrimination by heme proteins. J Biol Inorg Chem 8, 1-11.
    • (2003) J Biol Inorg Chem , vol.8 , pp. 1-11
    • Jain, R.1    Chan, M.K.2
  • 23
    • 2442624510 scopus 로고    scopus 로고
    • A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor
    • Kurokawa H, Lee DS, Watanabe M, Sagami I, Mikami B, Raman CS & Shimizu T (2004) A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor. J Biol Chem 279, 20189-20193.
    • (2004) J Biol Chem , vol.279 , pp. 20189-20193
    • Kurokawa, H.1    Lee, D.S.2    Watanabe, M.3    Sagami, I.4    Mikami, B.5    Raman, C.S.6    Shimizu, T.7
  • 24
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper SM, Neil LC & Gardner KH (2003) Structural basis of a phototropin light switch. Science 301, 1541-1544.
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 25
    • 0035853139 scopus 로고    scopus 로고
    • Structure of flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • Crosson S & Moffat K (2001) Structure of flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction. Proc Natl Acad Sci USA 98, 2995-3000.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 28
    • 0346734132 scopus 로고    scopus 로고
    • Structural basis for PAS domain heterodimerization in the basic-helix-loop-helix-PAS transcription factor hypoxia-inducible factor
    • Erbel PJA, Card PB, Karakuzu O, Bruick RK & Gardner KH (2003) Structural basis for PAS domain heterodimerization in the basic-helix-loop- helix-PAS transcription factor hypoxia-inducible factor. Proc Natl Acad Sci USA 100, 15504-15509.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15504-15509
    • Erbel, P.J.A.1    Card, P.B.2    Karakuzu, O.3    Bruick, R.K.4    Gardner, K.H.5
  • 29
    • 0036774056 scopus 로고    scopus 로고
    • Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation
    • Amezcua CA, Harper SM, Rutter J & Gardner KH (2002) Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation. Structure 10, 1349-1361.
    • (2002) Structure , vol.10 , pp. 1349-1361
    • Amezcua, C.A.1    Harper, S.M.2    Rutter, J.3    Gardner, K.H.4
  • 30
    • 0035544154 scopus 로고    scopus 로고
    • 15N chemical shift assignment of the N-terminal PAS domain of mNPAS2
    • 15N chemical shift assignment of the N-terminal PAS domain of mNPAS2. J Biomol NMR 21, 383-384.
    • (2001) J Biomol NMR , vol.21 , pp. 383-384
    • Holdeman, T.C.1    Gardner, K.H.2
  • 31
    • 20444374458 scopus 로고    scopus 로고
    • CO-dependent activity controlling mechanism of heme-containing CO-sensor protein, NPAS2
    • Uchida T, Sato E, Sato A, Sagami I, Shimizu T & Kitagawa T (2005) CO-dependent activity controlling mechanism of heme-containing CO-sensor protein, NPAS2. J Biol Chem 280, 21358-21368.
    • (2005) J Biol Chem , vol.280 , pp. 21358-21368
    • Uchida, T.1    Sato, E.2    Sato, A.3    Sagami, I.4    Shimizu, T.5    Kitagawa, T.6
  • 32
    • 1542327658 scopus 로고    scopus 로고
    • Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH)
    • Park H, Suquet C, Satterlee JD & Kang CH (2004) Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH). Biochemistry 43, 2738-2746.
    • (2004) Biochemistry , vol.43 , pp. 2738-2746
    • Park, H.1    Suquet, C.2    Satterlee, J.D.3    Kang, C.H.4
  • 33
    • 15444362702 scopus 로고    scopus 로고
    • Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling
    • Key J & Moffat K (2005) Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling. Biochemistry 44, 4627-4635.
    • (2005) Biochemistry , vol.44 , pp. 4627-4635
    • Key, J.1    Moffat, K.2
  • 34
    • 0346732270 scopus 로고    scopus 로고
    • Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: A study of deletion and site-directed mutants
    • Yoshimura T, Sagami I, Sasakura Y & Shimizu T (2003) Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: a study of deletion and site-directed mutants. J Biol Chem 278, 53105-53111.
    • (2003) J Biol Chem , vol.278 , pp. 53105-53111
    • Yoshimura, T.1    Sagami, I.2    Sasakura, Y.3    Shimizu, T.4


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