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CFP ‐1 interacts with HDAC 1/2 complexes in C. elegans development
Author(s) -
Pokhrel Bharat,
Chen Yannic,
Biro Jonathan Joseph
Publication year - 2019
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14833
Subject(s) - caenorhabditis elegans , biology , microbiology and biotechnology , genetics , gene , epigenetics , function (biology) , hdac1 , mutant , model organism , histone deacetylase , histone
CXXC finger binding protein 1 ( CFP ‐1) is an evolutionarily conserved protein that binds to non‐methylated CpG‐rich promoters in mammals and Caenorhabditis elegans . This conserved epigenetic regulator is part of the COMPASS complex that contains the H3K4me3 methyltransferase SET 1 in mammals and SET ‐2 in C. elegans . Previous studies have indicated the importance of CFP1 in embryonic stem cell differentiation and cell fate specification. However, neither the function nor the mechanism of action of CFP1 is well understood at the organismal level. Here, we have used cfp‐1(tm6369) and set‐2(bn129) C. elegans mutants to investigate the function of CFP ‐1 in gene induction and development. We have characterised C. elegans COMPASS mutants cfp‐1(tm6369) and set‐2(bn129) and found that both cfp‐1 and set‐2 play an important role in the regulation of fertility and development of the organism. Furthermore, we found that both cfp‐1 and set‐2 are required for H3K4 trimethylation and play a repressive role in the expression of heat shock and salt‐inducible genes. Interestingly, we found that cfp‐1 but not set‐2 genetically interacts with histone deacetylase ( HDAC 1/2) complexes to regulate fertility, suggesting a function of CFP ‐1 outside of the COMPASS complex. Additionally, we found that cfp‐1 and set‐2 independently regulate fertility and development of the organism. Our results suggest that CFP ‐1 genetically interacts with HDAC 1/2 complexes to regulate fertility, independent of its function within the COMPASS complex. We propose that CFP ‐1 could cooperate with the COMPASS complex and/or HDAC 1/2 in a context‐dependent manner.