Interaction of the λ-cro repressor protein with operator DNA fragments monitored as to amide proton magnetic resonances

Masahiro Shirakawa; Sang Jong Lee; Misato Takimoto; Hiroshi Matsuo; Hideo Akutsu; Yoshimasa Kyogoku

doi:10.1016/0022-2860(91)87147-A

Interaction of the λ-cro repressor protein with operator DNA fragments monitored as to amide proton magnetic resonances

Masahiro Shirakawa, Sang Jong Lee, Misato Takimoto, Hiroshi Matsuo, Hideo Akutsu, Yoshimasa Kyogoku

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Abstract

The amide proton magnetic resonances of the λ-cro repressor protein have been examined. In order to assign them to specific amino acid residues, we labeled the cro protein by incorporating ¹⁵N-enriched leucine or ¹⁵N-enriched lysine and then conducted ¹H/¹⁵N heteronuclear multiquantum coherence (HMQC) spectroscopy of the labeled cro protein. The chemical shifts of the amide proton resonances were titrated by the addition of operator DNA fragments. From the behavior of the shifts on binding to the operator DNAs, the DNA binding surface of the cro protein has been deduced. On the basis of the results with DNAs with different base sequences, the origins of the specific and nonspecific interactions are discussed.

Original language	English (US)
Pages (from-to)	355-366
Number of pages	12
Journal	Journal of Molecular Structure
Volume	242
Issue number	C
DOIs	https://doi.org/10.1016/0022-2860(91)87147-A
State	Published - Jan 1991
Externally published	Yes

Bibliographical note

Funding Information:
This work was partly supported by a grant from the Ministry of Education, Science and Culture, and Special Coordination Funds of the Science and Technology Agency.

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10.1016/0022-2860(91)87147-A

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title = "Interaction of the λ-cro repressor protein with operator DNA fragments monitored as to amide proton magnetic resonances",

abstract = "The amide proton magnetic resonances of the λ-cro repressor protein have been examined. In order to assign them to specific amino acid residues, we labeled the cro protein by incorporating 15N-enriched leucine or 15N-enriched lysine and then conducted 1H/15N heteronuclear multiquantum coherence (HMQC) spectroscopy of the labeled cro protein. The chemical shifts of the amide proton resonances were titrated by the addition of operator DNA fragments. From the behavior of the shifts on binding to the operator DNAs, the DNA binding surface of the cro protein has been deduced. On the basis of the results with DNAs with different base sequences, the origins of the specific and nonspecific interactions are discussed.",

author = "Masahiro Shirakawa and {Jong Lee}, Sang and Misato Takimoto and Hiroshi Matsuo and Hideo Akutsu and Yoshimasa Kyogoku",

note = "Funding Information: This work was partly supported by a grant from the Ministry of Education, Science and Culture, and Special Coordination Funds of the Science and Technology Agency.",

year = "1991",

month = jan,

doi = "10.1016/0022-2860(91)87147-A",

language = "English (US)",

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journal = "Journal of Molecular Structure",

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T1 - Interaction of the λ-cro repressor protein with operator DNA fragments monitored as to amide proton magnetic resonances

AU - Shirakawa, Masahiro

AU - Jong Lee, Sang

AU - Takimoto, Misato

AU - Matsuo, Hiroshi

AU - Akutsu, Hideo

AU - Kyogoku, Yoshimasa

N1 - Funding Information: This work was partly supported by a grant from the Ministry of Education, Science and Culture, and Special Coordination Funds of the Science and Technology Agency.

PY - 1991/1

Y1 - 1991/1

N2 - The amide proton magnetic resonances of the λ-cro repressor protein have been examined. In order to assign them to specific amino acid residues, we labeled the cro protein by incorporating 15N-enriched leucine or 15N-enriched lysine and then conducted 1H/15N heteronuclear multiquantum coherence (HMQC) spectroscopy of the labeled cro protein. The chemical shifts of the amide proton resonances were titrated by the addition of operator DNA fragments. From the behavior of the shifts on binding to the operator DNAs, the DNA binding surface of the cro protein has been deduced. On the basis of the results with DNAs with different base sequences, the origins of the specific and nonspecific interactions are discussed.

AB - The amide proton magnetic resonances of the λ-cro repressor protein have been examined. In order to assign them to specific amino acid residues, we labeled the cro protein by incorporating 15N-enriched leucine or 15N-enriched lysine and then conducted 1H/15N heteronuclear multiquantum coherence (HMQC) spectroscopy of the labeled cro protein. The chemical shifts of the amide proton resonances were titrated by the addition of operator DNA fragments. From the behavior of the shifts on binding to the operator DNAs, the DNA binding surface of the cro protein has been deduced. On the basis of the results with DNAs with different base sequences, the origins of the specific and nonspecific interactions are discussed.

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JO - Journal of Molecular Structure

JF - Journal of Molecular Structure

IS - C

ER -

Interaction of the λ-cro repressor protein with operator DNA fragments monitored as to amide proton magnetic resonances

Abstract

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