Unknown,Transcriptomics,Genomics,Proteomics

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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. Mechanistically, PHF20 is not required for maintaining the global H4K16 acetylation levels, but instead works downstream in transcriptional regulation of MOF target genes. ChIP sequencing of H4K16ace ChIP DNA from PHF20 knockout and wild type cells using Illumina Solexa Genome Analyzer II single end sequencing protocol.

ORGANISM(S): Mus musculus

SUBMITTER: kaifu chen 

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

REPOSITORIES: biostudies-arrayexpress

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Loss of the methyl lysine effector protein PHF20 impacts the expression of genes regulated by the lysine acetyltransferase MOF.

Badeaux Aimee I AI   Yang Yanzhong Y   Cardenas Kim K   Vemulapalli Vidyasiri V   Chen Kaifu K   Kusewitt Donna D   Richie Ellen E   Li Wei W   Bedford Mark T MT  

The Journal of biological chemistry 20111109 1


In epigenetic signaling pathways, histone tails are heavily modified, resulting in the recruitment of effector molecules that can influence 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 (male absent on the first) histone acetyltransferase protein complex, suggesting it plays a role in the cross-talk between lysine methylation and histone acetylation. We sought to investigate  ...[more]

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