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. Author manuscript; available in PMC: 2018 Mar 27.
Published in final edited form as: Nature. 2016 Jun 30;534(7609):625–626. doi: 10.1038/534625a

Figure 1. Coordinated responses to mitochondrial stress.

Figure 1

Gene expression can be inhibited by the tight packaging of DNA as chromatin around histone proteins that are decorated with methyl groups at specific amino-acid residues. Two such repressive modifications are dubbed H3K9me2 and H3K27me3. Two studies5,6 reveal that mitochondrial stress triggers the unpackaging and expression of genes involved in a stress response called the UPRmt. Tian et al.5 find that movement of the protein LIN-65 from the cytoplasm to the nucleus triggers nuclear migration of the transcription factor DVE-1. The enzyme MET2 mediates the addition of H3K9me2 modifications to histones in the cytoplasm; these histones move to the nucleus, restricting the unpackaged regions where DVE-1 can bind to promote transcription. Merkwirth et al.6 show that JMJD-1.2 and JMJD-3.1 enzymes are upregulated in response to mitochondrial stress and remove methyl groups from H3K27me3 to form the transcription-promoting modification H3K27me1 in the vicinity of UPRmt genes.