DNA G-quartets in a 1.86 Å resolution structure of an Oxytricha nova telomeric protein-DNA complex
The Oxytricha nova telomere end binding protein (OnTEBP) recognizes, binds and protects the single-stranded 3′-terminal DNA extension found at the ends of macronuclear chromosomes. The structure of this complex shows that the single strand GGGGTTTTGGGG DNA binds in a deep cleft between the two prote...
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Veröffentlicht in: | Journal of molecular biology 2001-07, Vol.310 (2), p.367-377 |
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Sprache: | eng |
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Oxytricha nova telomere end binding protein (OnTEBP) recognizes, binds and protects the single-stranded 3′-terminal DNA extension found at the ends of macronuclear chromosomes. The structure of this complex shows that the single strand GGGGTTTTGGGG DNA binds in a deep cleft between the two protein subunits of OnTEBP, adopting a non-helical and irregular conformation. In extending the resolution limit of this structure to 1.86 Å, we were surprised to find a G-quartet linked dimer of the GGGGTTTTGGGG DNA also packing within the crystal lattice and interacting with the telomere end binding protein. The G-quartet DNA exhibits the same structure and topology as previously observed in solution by NMR with diagonally crossing d(TTTT) loops at either end of the four-stranded helix. Additionally, the crystal structure reveals clearly visible Na
+, and specific patterns of bound water molecules in the four non-equivalent grooves. Although the G-quartet:protein contact surfaces are modest and might simply represent crystal packing interactions, it is interesting to speculate that the two types of telomeric DNA-protein interactions observed here might both be important in telomere biology. |
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ISSN: | 0022-2836 1089-8638 |
DOI: | 10.1006/jmbi.2001.4766 |