Proton NMR study on a type II DNA binding protein huα from escherichia coli and its complex with oligo DNA

H. Shindo; H. Kurumizaka; A. Furubayashi; C. Sakuma; U. Matumoto; A. Yanagida; N. Goshima; Y. Kano; F. Imamoto

doi:10.2116/analsci.7.Supple_849

Proton NMR study on a type II DNA binding protein huα from escherichia coli and its complex with oligo DNA

H. Shindo, H. Kurumizaka, A. Furubayashi, C. Sakuma, U. Matumoto, A. Yanagida, N. Goshima, Y. Kano, F. Imamoto

Research output: Contribution to journal › Article › peer-review

Abstract

The solution structures of HUα and its complex with oligo DNA were studied by proton NMR spectroscopy. It was confirmed that the arm region of HU forms antiparallel β-sheet and that all of the residues of phenylalanines together with some of leucines and/or valines form a hydrophobic core within the dimer of HU protein. Upon complex formation of HUα with DNA, several resonances from both HU and DNA were perturbed and the intermolecuar NOEs between HU and DNA were observed, suggesting that HU binds primarily to the minor groove of DNA.

Original language	English
Pages (from-to)	849-852
Number of pages	4
Journal	Analytical Sciences
Volume	7
Issue number	Supplement
DOIs	https://doi.org/10.2116/analsci.7.Supple_849
Publication status	Published - 1991
Externally published	Yes

Keywords

HU protein
NMR
protein complex with DNA

ASJC Scopus subject areas

Analytical Chemistry

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10.2116/analsci.7.Supple_849

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abstract = "The solution structures of HUα and its complex with oligo DNA were studied by proton NMR spectroscopy. It was confirmed that the arm region of HU forms antiparallel β-sheet and that all of the residues of phenylalanines together with some of leucines and/or valines form a hydrophobic core within the dimer of HU protein. Upon complex formation of HUα with DNA, several resonances from both HU and DNA were perturbed and the intermolecuar NOEs between HU and DNA were observed, suggesting that HU binds primarily to the minor groove of DNA.",

keywords = "HU protein, NMR, protein complex with DNA",

author = "H. Shindo and H. Kurumizaka and A. Furubayashi and C. Sakuma and U. Matumoto and A. Yanagida and N. Goshima and Y. Kano and F. Imamoto",

year = "1991",

doi = "10.2116/analsci.7.Supple_849",

language = "English",

volume = "7",

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journal = "Analytical Sciences",

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TY - JOUR

T1 - Proton NMR study on a type II DNA binding protein huα from escherichia coli and its complex with oligo DNA

AU - Shindo, H.

AU - Kurumizaka, H.

AU - Furubayashi, A.

AU - Sakuma, C.

AU - Matumoto, U.

AU - Yanagida, A.

AU - Goshima, N.

AU - Kano, Y.

AU - Imamoto, F.

PY - 1991

Y1 - 1991

N2 - The solution structures of HUα and its complex with oligo DNA were studied by proton NMR spectroscopy. It was confirmed that the arm region of HU forms antiparallel β-sheet and that all of the residues of phenylalanines together with some of leucines and/or valines form a hydrophobic core within the dimer of HU protein. Upon complex formation of HUα with DNA, several resonances from both HU and DNA were perturbed and the intermolecuar NOEs between HU and DNA were observed, suggesting that HU binds primarily to the minor groove of DNA.

AB - The solution structures of HUα and its complex with oligo DNA were studied by proton NMR spectroscopy. It was confirmed that the arm region of HU forms antiparallel β-sheet and that all of the residues of phenylalanines together with some of leucines and/or valines form a hydrophobic core within the dimer of HU protein. Upon complex formation of HUα with DNA, several resonances from both HU and DNA were perturbed and the intermolecuar NOEs between HU and DNA were observed, suggesting that HU binds primarily to the minor groove of DNA.

KW - HU protein

KW - NMR

KW - protein complex with DNA

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JO - Analytical Sciences

JF - Analytical Sciences

IS - Supplement

ER -

Proton NMR study on a type II DNA binding protein huα from escherichia coli and its complex with oligo DNA

Abstract

Keywords

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