TAILIEUCHUNG - Báo cáo khoa học: Spectroscopic characterization of the isolated heme-bound PAS-B domain of neuronal PAS domain protein 2 associated with circadian rhythms

Neuronal PAS domain protein 2 (NPAS2) is an important transcription factor associated with circadian rhythms. This protein forms a heterodimer with BMAL1, which binds to the E-box sequence to mediate circadian rhythm-regulated transcription. NPAS2 has two PAS domains with heme-binding sites in the N-terminal portion. In this study, we overexpressed wild-type and His mutants of the PAS-B domain (residues 241–416) of mouse NPAS2 and then purified and characterized the isolated heme-bound proteins | ềFEBS Journal Spectroscopic characterization of the isolated heme-bound PAS-B domain of neuronal PAS domain protein 2 associated with circadian rhythms Ryoji Koudo1 Hirofumi Kurokawa1 Emiko Sato1 Jotaro Igarashi1 Takeshi Uchida2 Ikuko Sagami1 Teizo Kitagawa2 and Toru Shimizu1 1 Institute of Multidisciplinary Research for Advanced Materials Tohoku University Sendai Japan 2 Okazaki Institute for Integrative Bioscience NationalInstitutes of NaturalSciences Okazaki Japan Keywords circadian rhythms heme-sensor protein PAS domain resonance Raman spectroscopy transcription Correspondence T. Shimizu Institute of Multidisciplinary Research for Advanced Materials Tohoku University 2-1-1 Katahira Aoba-ku Sendai 980-8577 Japan Fax 81 22 217 5604 5390 Tel 81 22 217 5604 5605 E-mail shimizu@ Present address Graduate Schoolof Agriculture Kyoto PrefecturalUniversity Nakaragi-cho 1-5 Shimogamo Sakyo-ku Kyoto 606-8522 Japan Received 24 March 2005 revised 15 June 2005 accepted 20 June 2005 doi Neuronal PAS domain protein 2 NPAS2 is an important transcription factor associated with circadian rhythms. This protein forms a heterodimer with BMAL1 which binds to the E-box sequence to mediate circadian rhythm-regulated transcription. NPAS2 has two PAS domains with hemebinding sites in the N-terminal portion. In this study we overexpressed wild-type and His mutants of the PAS-B domain residues 241-416 of mouse NPAS2 and then purified and characterized the isolated hemebound proteins. Optical absorption spectra of the wild-type protein showed that the Fe III Fe II and Fe II -CO complexes are 6-co-ordinated low-spin complexes. On the other hand resonance Raman spectra indicated that both the Fe III and Fe II complexes contain mixtures of 5-co-ordi-nated high-spin and 6-co-ordinated low-spin complexes. Based on inverse correlation between vFe-CO and VC-O of the resonance Raman spectra it appeared that the axial ligand trans to CO of the .

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