Details

Autor(en) / Beteiligte

• Shi, Xiaobing
• Kachirskaia, Ioulia
• Walter, Kay L.
• Kuo, Jen-Hao A.
• Lake, Aimee
• Davrazou, Foteini
• Chan, Steve M.
• Martin, David G.E.
• Fingerman, Ian M.
• Briggs, Scott D.
• Howe, LeAnn
• Utz, Paul J.
• Kutateladze, Tatiana G.
• Lugovskoy, Alexey A.
• Bedford, Mark T.
• Gozani, Or

Titel

Proteome-wide Analysis in Saccharomyces cerevisiae Identifies Several PHD Fingers as Novel Direct and Selective Binding Modules of Histone H3 Methylated at Either Lysine 4 or Lysine 36

Ist Teil von

• The Journal of biological chemistry, 2007-01, Vol.282 (4), p.2450-2455

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2007

Quelle

Electronic Journals Library

Beschreibungen/Notizen

• The PHD finger motif is a signature chromatin-associated motif that is found throughout eukaryotic proteomes. Here we have determined the histone methyl-lysine binding activity of the PHD fingers present within the Saccharomyces cerevisiae proteome. We provide evidence on the genomic scale that PHD fingers constitute a general class of effector modules for histone H3 trimethylated at lysine 4 (H3K4me3) and histone H3 trimethylated at lysine 36 (H3K36me3). Structural modeling of PHD fingers demonstrates a conserved mechanism for recognizing the trimethyl moiety and provides insight into the molecular basis of affinity for the different methyl-histone ligands. Together, our study suggests that a common function for PHD fingers is to transduce methyl-lysine events and sheds light on how a single histone modification can be linked to multiple biological outcomes.