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
| Autor: | LeAnn J. Howe, Kay L. Walter, Xiaobing Shi, Steve M. Chan, Paul J. Utz, Alexey Lugovskoy, Aimee Lake, Jen Hao A. Kuo, Mark T. Bedford, Scott D. Briggs, Foteini Davrazou, David G. E. Martin, Or Gozani, Tatiana G. Kutateladze, Ian M. Fingerman, Ioulia Kachirskaia |
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| Rok vydání: | 2006 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Proteome education Amino Acid Motifs Molecular Sequence Data Saccharomyces cerevisiae Biochemistry Methylation Article Histones Histone H3 hemic and lymphatic diseases Histone H2A Histone code Histone octamer Amino Acid Sequence Molecular Biology health care economics and organizations Homeodomain Proteins biology Lysine Cell Biology Protein Structure Tertiary DNA-Binding Proteins Histone PHD finger Histone methyltransferase biology.protein H3K4me3 Protein Binding |
| Zdroj: | The Journal of biological chemistry. 282(4) |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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