![]()
|
|
||||||||
J Biol Chem, Vol. 273, Issue 32, 19988-19992, August 7, 1998
From the Department of Molecular Engineering, Graduate School of
Engineering, Kyoto University, Kyoto 606-8501, Japan
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 cm
Heme Environmental Structure of CooA Is Modulated by the Target
DNA Binding
EVIDENCE FROM RESONANCE RAMAN SPECTROSCOPY AND CO REBINDING
KINETICS
1, 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 cm
1 and
narrowing of the main line at 486 cm
1 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.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
![]()
CiteULike
Complore
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
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] |
||||
![]() |
F. J. M. Chartier and M. Couture Stability of the Heme Environment of the Nitric Oxide Synthase from Staphylococcus aureus in the Absence of Pterin Cofactor Biophys. J., September 1, 2004; 87(3): 1939 - 1950. [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] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |