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The structure of the Holliday junction, and its resolution.

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Diekmann,  S.
Abteilung Kinetik der Phasenbildung, MPI for biophysical chemistry, Max Planck Society;

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von Kitzing,  E.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Duckett, D. R., Murchie, A. I. H., Diekmann, S., von Kitzing, E., Kemper, B., & Lilley, D. M. J. (1988). The structure of the Holliday junction, and its resolution. Cell, 55(1), 79-89. doi:10.1016/0092-8674(88)90011-6.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-42E6-2
Abstract
The Holliday (four-way) junction is a critical intermediate in homologous genetic recombination. We have studied the structure of a series of four-way junctions, constructed by hybridization of four 80 nucleotide synthetic oligonucleotides. These molecules migrate anomalously slowly in gel electrophoresis. Each arm of any junction could be selectively shortened by cleavage at a unique restriction site, and we have studied the relative gel mobilities of species in which two arms were cleaved. The pattern of fragments observed argues strongly for a structure with two-fold symmetry, based on an X shape, the long arms of which are made from pairwise colinear association of helical arms. The choice of partners is governed by the base sequence at the junction, allowing a potential isomerization between equivalent structural forms. Resolvase enzymes can distinguish between these structures, and the resolution products are determined by the structure adopted, i.e., by the sequence at the junction. In the absence of cations, the helical arms of the junction are fully extended in a square configuration, and unstacking results in junction thymines becoming reactive to osmium tetroxide.