The paper:
J. Wysocka et al., "WDR5 associates with histone H3 methylated K4 and is essential for H3K4 methylation and vertebrate development," Cell, 121:859-72, 2005. (Cited in 96 papers)
The finding:
David Allis from Rockefeller University and colleagues used a biochemical pull-down assay and found that the protein WDR5, a common part of histone methyltransferase complexes, associates specifically with dimethylated H3K4 nucleosomes. The absence of WDR5 in tadpoles resulted in developmental defects and abnormal Hox gene expression.
The significance:
"The paper at the time was very provocative," says Danny Reinberg of the Robert Wood Johnson Medical School in New Jersey, because it was the first to tie vertebrate development to the recognition of a specific histone modification.
The contradiction:
Three separate studies, including one by Allis and colleagues, later indicated that the specificity of WDR5 for dimethylated H3K4 is "plain wrong," Reinberg says. WDR5 bound "with almost no difference" in ...
