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 journalArticle

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 languageEnglish
Pages (from-to)849-852
Number of pages4
JournalAnalytical Sciences
Volume7
Issue numberSupplement
DOIs
Publication statusPublished - 1991
Externally publishedYes

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Keywords

  • HU protein
  • NMR
  • protein complex with DNA

ASJC Scopus subject areas

  • Analytical Chemistry

Cite this

Shindo, H., Kurumizaka, H., Furubayashi, A., Sakuma, C., Matumoto, U., Yanagida, A., Goshima, N., Kano, Y., & Imamoto, F. (1991). Proton NMR study on a type II DNA binding protein huα from escherichia coli and its complex with oligo DNA. Analytical Sciences, 7(Supplement), 849-852. https://doi.org/10.2116/analsci.7.Supple_849