Disease relevance of YNG1

• Using the toxicity of YNG1 overexpression as a tool, we showed that Yng1p interacts with the amino-terminal tail of histone H3 and that this interaction can be disrupted by loss of lysine 4 methylation within this tail [1].

High impact information on YNG1

• There are three members of the ING family in Saccharomyces cerevisiae: Yng1p, Yng2p, and Pho23p [1].
• The yng1p plant homeodomain finger is a methyl-histone binding module that recognizes lysine 4-methylated histone h3 [1].
• Additionally, we mapped the region of Yng1p required for overexpression of toxicity to the PHD finger, showed that this region capable of binding lysine 4-methylated histone H3 in vitro, and demonstrated that mutations of the PHD finger that abolish binding in vitro are no longer toxic in vivo [1].
• These results identify a novel function for the Yng1p PHD finger in promoting stabilization of the NuA3 complex at chromatin through recognition of histone H3 lysine 4 methylation [1].
• Instead, we find that Yng1p mediates the interaction of Sas3p with nucleosomes and is thus required for the ability of NuA3 to modify histone tails [2].

Biological context of YNG1

• Surprisingly, deletion of YNG1 or SAS3 leads to increased transcriptional activation by p53 [3].
• Yng1- and Pho23-deficient cells also share some of these phenotypes [4].
• Yng1p is a stable component of the NuA3 histone acetyltransferase complex, which contains Sas3p, the yeast homolog of the mammalian MOZ proto-oncogene product, as its catalytic subunit [2].

Other interactions of YNG1

• We further demonstrated by coimmunoprecipitation that HA-Yng1, HA-Yng2, HA-Pho23, and HA-Ing1 are associated with HAT activities in yeast [4].

References