Deciphering and engineering chromodomain-methyllysine peptide recognition
نویسندگان
چکیده
منابع مشابه
Identification of methyllysine peptides binding to chromobox protein homolog 6 chromodomain in the human proteome.
Methylation is one of the important post-translational modifications that play critical roles in regulating protein functions. Proteomic identification of this post-translational modification and understanding how it affects protein activity remain great challenges. We tackled this problem from the aspect of methylation mediating protein-protein interaction. Using the chromodomain of human chro...
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Recognition of methylated histone tail lysine residues by tudor domains plays important roles in epigenetic control of gene expression and DNA damage response. Previous studies revealed the binding of methyllysine in a cage of aromatic residues, but the molecular mechanism by which the sequence specificity for surrounding histone tail residues is achieved remains poorly understood. In the cryst...
متن کاملRecognition of methylated peptides by Drosophila melanogaster polycomb chromodomain.
Lysine methylation is one of the important post-translational modifications (PTMs) that regulate protein functions. Up to now, proteomic identification of this PTM remains a challenge due to the lack of effective enrichment methods in mass spectrometry experiments. To address this challenge, we present here a systematic approach to predicting peptides in which lysine residues may be methylated ...
متن کاملEngineering of double tudor domain and chromodomain variants with altered binding specificities
The first library we constructed and screened in this work (lib1) was composed of potential H3K27-trimethylation biosensors containing a variety of different binding domains. Among the binding domains included in this library were three engineered variants that have been developed in our lab and not previously reported elsewhere: JMJD2A double tudor domain [1,2] with D945K; JMJD2A double tudor ...
متن کاملSpecificity of the chromodomain Y chromosome family of chromodomains for lysine-methylated ARK(S/T) motifs.
Previous studies have shown two homologous chromodomain modules in the HP1 and Polycomb proteins exhibit discriminatory binding to related methyllysine residues (embedded in ARKS motifs) of the histone H3 tail. Methylated ARK(S/T) motifs have recently been identified in other chromatin factors (e.g. linker histone H1.4 and lysine methyltransferase G9a). These are thought to function as peripher...
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ژورنال
عنوان ژورنال: Science Advances
سال: 2018
ISSN: 2375-2548
DOI: 10.1126/sciadv.aau1447