Solution structure of CEH-37 homeodomain of the nematode Caenorhabditis elegans

Sunjin Moon, Yong Woo Lee, Woo Taek Kim, Weon Tae Lee

Research output: Contribution to journalArticle

Abstract

The nematode Caenorhabditis elegans protein CEH-37 belongs to the paired OTD/OTX family of homeobox-containing homeodomain proteins. CEH-37 shares sequence similarity with homeodomain proteins, although it specifically binds to double-stranded C. elegans telomeric DNA, which is unusual to homeodomain proteins. Here, we report the solution structure of CEH-37 homeodomain and molecular interaction with double-stranded C. elegans telomeric DNA using nuclear magnetic resonance (NMR) spectroscopy. NMR structure shows that CEH-37 homeodomain is composed of a flexible N-terminal region and three α-helices with a helix-turn-helix (HTH) DNA binding motif. Data from size-exclusion chromatography and fluorescence spectroscopy reveal that CEH-37 homeodomain interacts strongly with double-stranded C. elegans telomeric DNA. NMR titration experiments identified residues responsible for specific binding to nematode double-stranded telomeric DNA. These results suggest that C. elegans homeodomain protein, CEH-37 could play an important role in telomere function via DNA binding.

Original languageEnglish
Pages (from-to)370-375
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume443
Issue number2
DOIs
Publication statusPublished - 2014 Jan 10

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Caenorhabditis elegans
Homeodomain Proteins
Caenorhabditis elegans Proteins
DNA
Magnetic Resonance Spectroscopy
Nucleotide Motifs
Nuclear magnetic resonance
Homeobox Genes
Fluorescence Spectrometry
Telomere
Molecular interactions
Size exclusion chromatography
Fluorescence spectroscopy
Gel Chromatography
Titration
Nuclear magnetic resonance spectroscopy
Experiments

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

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abstract = "The nematode Caenorhabditis elegans protein CEH-37 belongs to the paired OTD/OTX family of homeobox-containing homeodomain proteins. CEH-37 shares sequence similarity with homeodomain proteins, although it specifically binds to double-stranded C. elegans telomeric DNA, which is unusual to homeodomain proteins. Here, we report the solution structure of CEH-37 homeodomain and molecular interaction with double-stranded C. elegans telomeric DNA using nuclear magnetic resonance (NMR) spectroscopy. NMR structure shows that CEH-37 homeodomain is composed of a flexible N-terminal region and three α-helices with a helix-turn-helix (HTH) DNA binding motif. Data from size-exclusion chromatography and fluorescence spectroscopy reveal that CEH-37 homeodomain interacts strongly with double-stranded C. elegans telomeric DNA. NMR titration experiments identified residues responsible for specific binding to nematode double-stranded telomeric DNA. These results suggest that C. elegans homeodomain protein, CEH-37 could play an important role in telomere function via DNA binding.",
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Solution structure of CEH-37 homeodomain of the nematode Caenorhabditis elegans. / Moon, Sunjin; Lee, Yong Woo; Kim, Woo Taek; Lee, Weon Tae.

In: Biochemical and Biophysical Research Communications, Vol. 443, No. 2, 10.01.2014, p. 370-375.

Research output: Contribution to journalArticle

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