Identification of the region in Escherichia coli DnaA protein required for specific recognition of the DnaA box
Y. Yoshida, T. Obita, Y. Kokusho, T. Ohmura, Tsutomu Katayama, Tadashi Ueda, T. Imoto
Pharmaceutical Health Care and Sciences
DnaA protein binds specifically to a 9-base-pair motif called the DnaA box. Domain IV comprises 94 amino acid residues and is required for DNA binding. Using nuclear magnetic resonance analysis, we investigated the interaction between DnaA domain IV and both a DnaA box and a non-specific oligonucleotide that has a reduced affinity for DnaA. The 1H-15N HSQC spectrum of DnaA domain IV showed prominent chemical shift perturbations on six residues (Arg399, Ala404, Leu422, Asp433, Thr435 and Thr436) in the presence of the DnaA box. Through homology modeling, we located all of these residues on one side surface of the DnaA domain IV molecule. Moreover, we compared the chemical shift perturbation of the 1H-15N HSQC spectrum in the presence of the DnaA box with that in the presence of a non-specific oligonucleotide, and the results suggested that Leu422 imparts specificity in binding with the DnaA box.
Cellular and Molecular Life Sciences
Escherichia coli Proteins
Chemical shift
Base Pairing
Yoshida, Y., Obita, T., Kokusho, Y., Ohmura, T., Katayama, T., Ueda, T., & Imoto, T. (2003). Identification of the region in Escherichia coli DnaA protein required for specific recognition of the DnaA box. Cellular and Molecular Life Sciences, 60(9), 1998-2008. https://doi.org/10.1007/s00018-003-3176-7
Identification of the region in Escherichia coli DnaA protein required for specific recognition of the DnaA box. / Yoshida, Y.; Obita, T.; Kokusho, Y.; Ohmura, T.; Katayama, Tsutomu; Ueda, Tadashi; Imoto, T.
In: Cellular and Molecular Life Sciences, Vol. 60, No. 9, 01.09.2003, p. 1998-2008.
Yoshida, Y, Obita, T, Kokusho, Y, Ohmura, T, Katayama, T, Ueda, T & Imoto, T 2003, 'Identification of the region in Escherichia coli DnaA protein required for specific recognition of the DnaA box', Cellular and Molecular Life Sciences, vol. 60, no. 9, pp. 1998-2008. https://doi.org/10.1007/s00018-003-3176-7
Yoshida Y, Obita T, Kokusho Y, Ohmura T, Katayama T, Ueda T et al. Identification of the region in Escherichia coli DnaA protein required for specific recognition of the DnaA box. Cellular and Molecular Life Sciences. 2003 Sep 1;60(9):1998-2008. https://doi.org/10.1007/s00018-003-3176-7
Yoshida, Y. ; Obita, T. ; Kokusho, Y. ; Ohmura, T. ; Katayama, Tsutomu ; Ueda, Tadashi ; Imoto, T. / Identification of the region in Escherichia coli DnaA protein required for specific recognition of the DnaA box. In: Cellular and Molecular Life Sciences. 2003 ; Vol. 60, No. 9. pp. 1998-2008.
@article{04f3f60ed2f0458d8105e89c81761d9f,
title = "Identification of the region in Escherichia coli DnaA protein required for specific recognition of the DnaA box",
abstract = "DnaA protein binds specifically to a 9-base-pair motif called the DnaA box. Domain IV comprises 94 amino acid residues and is required for DNA binding. Using nuclear magnetic resonance analysis, we investigated the interaction between DnaA domain IV and both a DnaA box and a non-specific oligonucleotide that has a reduced affinity for DnaA. The 1H-15N HSQC spectrum of DnaA domain IV showed prominent chemical shift perturbations on six residues (Arg399, Ala404, Leu422, Asp433, Thr435 and Thr436) in the presence of the DnaA box. Through homology modeling, we located all of these residues on one side surface of the DnaA domain IV molecule. Moreover, we compared the chemical shift perturbation of the 1H-15N HSQC spectrum in the presence of the DnaA box with that in the presence of a non-specific oligonucleotide, and the results suggested that Leu422 imparts specificity in binding with the DnaA box.",
author = "Y. Yoshida and T. Obita and Y. Kokusho and T. Ohmura and Tsutomu Katayama and Tadashi Ueda and T. Imoto",
journal = "Cellular and Molecular Life Sciences",
publisher = "Birkhauser Verlag Basel",
T1 - Identification of the region in Escherichia coli DnaA protein required for specific recognition of the DnaA box
AU - Yoshida, Y.
AU - Obita, T.
AU - Kokusho, Y.
AU - Ohmura, T.
AU - Katayama, Tsutomu
AU - Ueda, Tadashi
AU - Imoto, T.
N2 - DnaA protein binds specifically to a 9-base-pair motif called the DnaA box. Domain IV comprises 94 amino acid residues and is required for DNA binding. Using nuclear magnetic resonance analysis, we investigated the interaction between DnaA domain IV and both a DnaA box and a non-specific oligonucleotide that has a reduced affinity for DnaA. The 1H-15N HSQC spectrum of DnaA domain IV showed prominent chemical shift perturbations on six residues (Arg399, Ala404, Leu422, Asp433, Thr435 and Thr436) in the presence of the DnaA box. Through homology modeling, we located all of these residues on one side surface of the DnaA domain IV molecule. Moreover, we compared the chemical shift perturbation of the 1H-15N HSQC spectrum in the presence of the DnaA box with that in the presence of a non-specific oligonucleotide, and the results suggested that Leu422 imparts specificity in binding with the DnaA box.
AB - DnaA protein binds specifically to a 9-base-pair motif called the DnaA box. Domain IV comprises 94 amino acid residues and is required for DNA binding. Using nuclear magnetic resonance analysis, we investigated the interaction between DnaA domain IV and both a DnaA box and a non-specific oligonucleotide that has a reduced affinity for DnaA. The 1H-15N HSQC spectrum of DnaA domain IV showed prominent chemical shift perturbations on six residues (Arg399, Ala404, Leu422, Asp433, Thr435 and Thr436) in the presence of the DnaA box. Through homology modeling, we located all of these residues on one side surface of the DnaA domain IV molecule. Moreover, we compared the chemical shift perturbation of the 1H-15N HSQC spectrum in the presence of the DnaA box with that in the presence of a non-specific oligonucleotide, and the results suggested that Leu422 imparts specificity in binding with the DnaA box.
JO - Cellular and Molecular Life Sciences
JF - Cellular and Molecular Life Sciences