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Heterochromatin and associated gene silencing processes play roles in development, genome defense, and chromosome function. In many species, constitutive heterochromatin is decorated with histone H3 tri-methylated at lysine 9 (H3K9me3) and cytosine methylation. In  Neurospora crassa , a five-protein complex, DCDC, catalyzes H3K9 methylation, which then directs DNA methylation. Here, we identify and characterize a gene important for DCDC function,  dim-3  ( d efective  i n  m ethylation-3), which encodes the nuclear import chaperone NUP-6 (Importin α). The critical mutation in  dim-3  results in a substitution in an ARM repeat of NUP-6 and causes a substantial loss of H3K9me3 and DNA methylation. Surprisingly, nuclear transport of all known proteins involved in histone and DNA methylation, as well as a canonical transport substrate, appear normal in  dim-3  strains. Interactions between DCDC members also appear normal, but the  nup-6dim-3  allele causes the DCDC members DIM-5 and DIM-7 to mislocalize from heterochromatin and NUP-6  dim-3   itself is mislocalized from the nuclear envelope, at least in conidia. GCN-5, a member of the SAGA histone acetyltransferase complex, also shows altered localization in  dim-3 , raising the possibility that NUP-6 is necessary to localize multiple chromatin complexes following nucleocytoplasmic transport.

Neurospora Importin α Is Required for Normal Heterochromatic Formation and DNA Methylation