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Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions

Creator: Shanle, Erin K, Shinsky, Stephen A, Bridgers, Joseph B, Bae, Narkhyun, Sagum, Cari, Krajewski, Krzysztof, Rothbart, Scott B, Bedford, Mark T, Strahl, Brian

Abstract Background Histone posttranslational modifications (PTMs) function to regulate chromatin structure and function in part through the recruitment of effector proteins that harbor specialized “reader” domains. Despite efforts to elucidate (more)

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13072_2017_article_117.pdf

Collection: BioMed Central

Date Deposited: 2017-03-17

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Additional file 1: Table S1. Protein domains screened by histone peptide microarray

Collection: BioMed Central

Date Deposited: 2017-03-17

Date Created: 2017-03-17

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Additional file 2: Table S2. Histone peptide library used for peptide microarrays

Collection: BioMed Central

Date Deposited: 2017-03-17

Date Created: 2017-03-17

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Additional file 3: Figure S1. SPIN1 Tudor domain interaction with H3K4me3 and H4K20me3

Collection: BioMed Central

Date Deposited: 2017-03-17

Date Created: 2017-03-17

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Additional file 4: Figure S2. Peptide microarray data for SGF29 and Taf3

Collection: BioMed Central

Date Deposited: 2017-03-17

Date Created: 2017-03-17

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Additional file 5: Figure S3. CHD1 chromodomain histone peptide microarray

Collection: BioMed Central

Date Deposited: 2017-03-17

Date Created: 2017-03-17

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Additional file 6: Figure S4. CHD7 chromodomain histone peptide microarray

Collection: BioMed Central

Date Deposited: 2017-03-17

Date Created: 2017-03-17

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Additional file 7: Figure S5. CHD9 chromodomain histone peptide microarray

Collection: BioMed Central

Date Deposited: 2017-03-17

Date Created: 2017-03-17

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Additional file 8: Figure S6. TDRD3 Tudor domain histone peptide microarray

Collection: BioMed Central

Date Deposited: 2017-03-17

Date Created: 2017-03-17

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