HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Uchida, T. Articles by Aono, S. Search for Related Content PubMed PubMed Citation Articles by Uchida, T. Articles by Aono, S. Social Bookmarking                      What's this?

J Biol Chem, Vol. 273, Issue 32, 19988-19992, August 7, 1998

Heme Environmental Structure of CooA Is Modulated by the Target DNA Binding
EVIDENCE FROM RESONANCE RAMAN SPECTROSCOPY AND CO REBINDING KINETICS

From the Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto 606-8501, Japan

Kei Ohkubo, Hiroshi Nakajima, and Shigetoshi Aono

From the School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Tatsunokuchi, Nomi-gun, Ishikawa 923-1292, Japan

In order to investigate the gene activation mechanism triggered by the CO binding to CooA, a heme-containing transcriptional activator, the heme environmental structure and the dynamics of the CO rebinding and dissociation have been examined in the absence and presence of its target DNA. In the absence of DNA, the Fe-CO and C=O stretching Raman lines of the CO-bound CooA were observed at 487 and 1969 cm¹, respectively, suggesting that a neutral histidine is an axial ligand trans to CO. The frequency of (Fe-CO) implies an open conformation of the distal heme pocket, indicating that the ligand replaced by CO is located away from the bound CO. When the target DNA was added to CO-bound CooA, an appearance of a new (Fe-CO) line at 519 cm¹ and narrowing of the main line at 486 cm¹ were observed. Although the rate of the CO dissociation was insensitive to the additions of DNA, the CO rebinding was decelerated in the presence of the target DNA, but not in the presence of nonsense DNA. These observations demonstrate the structural alterations in the heme distal site in response to binding of the target DNA and support the activation mechanism proposed for CooA, which is triggered by the movement of the heme distal ligand to modify the conformation of the DNA binding domain.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				M. Ibrahim, R. L. Kerby, M. Puranik, I. H. Wasbotten, H. Youn, G. P. Roberts, and T. G. Spiro Heme Displacement Mechanism of CooA Activation: MUTATIONAL AND RAMAN SPECTROSCOPIC EVIDENCE J. Biol. Chem., September 29, 2006; 281(39): 29165 - 29173. [Abstract] [Full Text] [PDF]

				M. Kubo, S. Inagaki, S. Yoshioka, T. Uchida, Y. Mizutani, S. Aono, and T. Kitagawa Evidence for Displacements of the C-helix by CO Ligation and DNA Binding to CooA Revealed by UV Resonance Raman Spectroscopy J. Biol. Chem., April 21, 2006; 281(16): 11271 - 11278. [Abstract] [Full Text] [PDF]

				T. Uchida, E. Sato, A. Sato, I. Sagami, T. Shimizu, and T. Kitagawa CO-dependent Activity-controlling Mechanism of Heme-containing CO-sensor Protein, Neuronal PAS Domain Protein 2 J. Biol. Chem., June 3, 2005; 280(22): 21358 - 21368. [Abstract] [Full Text] [PDF]

				H. Youn, M. V. Thorsteinsson, M. Conrad, R. L. Kerby, and G. P. Roberts Dual Roles of an E-Helix Residue, Glu167, in the Transcriptional Activator Function of CooA J. Bacteriol., April 15, 2005; 187(8): 2573 - 2581. [Abstract] [Full Text] [PDF]

				S. Inagaki, C. Masuda, T. Akaishi, H. Nakajima, S. Yoshioka, T. Ohta, B. Pal, T. Kitagawa, and S. Aono Spectroscopic and Redox Properties of a CooA Homologue from Carboxydothermus hydrogenoformans J. Biol. Chem., February 4, 2005; 280(5): 3269 - 3274. [Abstract] [Full Text] [PDF]

				T. Yamashita, Y. Hoashi, Y. Tomisugi, Y. Ishikawa, and T. Uno The C-helix in CooA Rolls upon CO Binding to Ferrous Heme J. Biol. Chem., November 5, 2004; 279(45): 47320 - 47325. [Abstract] [Full Text] [PDF]

				G. P. Roberts, H. Youn, and R. L. Kerby CO-Sensing Mechanisms Microbiol. Mol. Biol. Rev., September 1, 2004; 68(3): 453 - 473. [Abstract] [Full Text] [PDF]

				T. Yamashita, Y. Hoashi, K. Watanabe, Y. Tomisugi, Y. Ishikawa, and T. Uno Roles of Heme Axial Ligands in the Regulation of CO Binding to CooA J. Biol. Chem., May 14, 2004; 279(20): 21394 - 21400. [Abstract] [Full Text] [PDF]

				J. Igarashi, A. Sato, T. Kitagawa, T. Yoshimura, S. Yamauchi, I. Sagami, and T. Shimizu Activation of Heme-regulated Eukaryotic Initiation Factor 2{alpha} Kinase by Nitric Oxide Is Induced by the Formation of a Five-coordinate NO-Heme Complex: OPTICAL ABSORPTION, ELECTRON SPIN RESONANCE, AND RESONANCE RAMAN SPECTRAL STUDIES J. Biol. Chem., April 16, 2004; 279(16): 15752 - 15762. [Abstract] [Full Text] [PDF]

				S. Taguchi, T. Matsui, J. Igarashi, Y. Sasakura, Y. Araki, O. Ito, S. Sugiyama, I. Sagami, and T. Shimizu Binding of Oxygen and Carbon Monoxide to a Heme-regulated Phosphodiesterase from Escherichia coli: KINETICS AND INFRARED SPECTRA OF THE FULL-LENGTH WILD-TYPE ENZYME, ISOLATED PAS DOMAIN, AND MET-95 MUTANTS J. Biol. Chem., January 30, 2004; 279(5): 3340 - 3347. [Abstract] [Full Text] [PDF]

				C. M. Coyle, M. Puranik, H. Youn, S. B. Nielsen, R. D. Williams, R. L. Kerby, G. P. Roberts, and T. G. Spiro Activation Mechanism of the CO Sensor CooA: MUTATIONAL AND RESONANCE RAMAN SPECTROSCOPIC STUDIES J. Biol. Chem., September 12, 2003; 278(37): 35384 - 35393. [Abstract] [Full Text] [PDF]

				A. Sato, Y. Sasakura, S. Sugiyama, I. Sagami, T. Shimizu, Y. Mizutani, and T. Kitagawa Stationary and Time-resolved Resonance Raman Spectra of His77 and Met95 Mutants of the Isolated Heme Domain of a Direct Oxygen Sensor from Escherichia coli J. Biol. Chem., August 30, 2002; 277(36): 32650 - 32658. [Abstract] [Full Text] [PDF]

				S. Aono, T. Kato, M. Matsuki, H. Nakajima, T. Ohta, T. Uchida, and T. Kitagawa Resonance Raman and Ligand Binding Studies of the Oxygen-sensing Signal Transducer Protein HemAT from Bacillus subtilis J. Biol. Chem., April 12, 2002; 277(16): 13528 - 13538. [Abstract] [Full Text] [PDF]

				S. Aono, K. Ohkubo, T. Matsuo, and H. Nakajima Redox-controlled Ligand Exchange of the Heme in the CO-sensing Transcriptional Activator CooA J. Biol. Chem., October 2, 1998; 273(40): 25757 - 25764. [Abstract] [Full Text] [PDF]

				K. Yamamoto, H. Ishikawa, S. Takahashi, K. Ishimori, I. Morishima, H. Nakajima, and S. Aono Binding of CO at the Pro2 Side Is Crucial for the Activation of CO-sensing Transcriptional Activator CooA. 1H NMR SPECTROSCOPIC STUDIES J. Biol. Chem., April 6, 2001; 276(15): 11473 - 11476. [Abstract] [Full Text] [PDF]

				H. Nakajima, Y. Honma, T. Tawara, T. Kato, S.-Y. Park, H. Miyatake, Y. Shiro, and S. Aono Redox Properties and Coordination Structure of the Heme in the CO-sensing Transcriptional Activator CooA J. Biol. Chem., March 2, 2001; 276(10): 7055 - 7061. [Abstract] [Full Text] [PDF]

				S. Kumazaki, H. Nakajima, T. Sakaguchi, E. Nakagawa, H. Shinohara, K. Yoshihara, and S. Aono Dissociation and Recombination between Ligands and Heme in a CO-sensing Transcriptional Activator CooA. A FLASH PHOTOLYSIS STUDY J. Biol. Chem., December 1, 2000; 275(49): 38378 - 38383. [Abstract] [Full Text] [PDF]

				H. Nakajima, E. Nakagawa, K. Kobayashi, S.-i. Tagawa, and S. Aono Ligand-switching Intermediates for the CO-sensing Transcriptional Activator CooA Measured by Pulse Radiolysis J. Biol. Chem., October 5, 2001; 276(41): 37895 - 37899. [Abstract] [Full Text] [PDF]