Loss of PHF20 does not negatively affect deposition of H4K16 acetylation, but does impact the expression of MOF targets

ABSTRACT: Protein post-translational modifications transmit signals in part by creating binding sites for effector molecules. This is especially true in epigenetic pathways where histone tails are heavily modified, resulting in the recruitment of molecules that can affect transcription. One such molecule, plant homeodomain finger protein 20 (PHF20), uses a Tudor domain to read dimethyl-lysine residues and is a known component of the MOF histone acetyltransferase protein complex, suggesting it plays a role in the crosstalk between lysine methylation and histone acetylation. We sought to investigate the biological role of PHF20 by generating a knockout mouse. Without PHF20, mice die shortly after birth and display a wide variety of phenotypes within the skeletal and hematopoietic systems. Mechanistica

ORGANISM(S): Mus musculus

SUBMITTER: kaifu chen 

PROVIDER: E-GEOD-29306 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress