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Ed as either HECT domain or RING domain. Ubiquitin is directly conjugated to an internal cysteine residue of HECT domain E3's before being transferred onto the substrate protein [5]. RING E3's do not conjugate ubiquitin, but rather stimulate its transfer from the E2 to the substrate [6,7]. RING domains contain conserved cysteine and histidine residues that chelate zinc ions to provide a structure
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Tion via a thiolester linkage to an internal cysteine in E1, which then transfers the ubiquitin to a cysteine residue of an E2 protein. The E2 interacts with an E3 to mediate covalent attachment of ubiquitin onto substrate proteins. Repeated rounds of E2/E3mediated ubiquitin transfer result in polyubiquitylation, allowing substrate proteins to be recognized and destroyed by the proteasome. Vertebr
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For the Sry transgenic mice, R. Watkins (UCLA), R. Bijlani (UCLA), M. Cheng (UW), D. K. Nguyen (UW), N. Krakauer (UC Berkeley), and P. Mann (Tufts U) for technical and editorial assistance.Author ContributionsConceived and designed the experiments: CD JX. Performed the experiments: JX XD. Analyzed the data: CD JX XD. Wrote the paper: CD JX.Many aspects of cell and developmental biology requi
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The mouse tiling array (2006-07-17MM8 tiling_set38), which covers the second half of the X chromosome (ChrX:93,883,966- 165,556,020, UCSC mouse genome Feb 2006 assembly) and the complete Y chromosome, was used in this study to closely compare the H4K16 acetylation pattern between Jarid1c and Jarid1d present on the same array. Analysis was done using the manufacturer software.Supporting Information
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The mouse tiling array (2006-07-17MM8 tiling_set38), which covers the second half of the X chromosome (ChrX:93,883,966- 165,556,020, UCSC mouse genome Feb 2006 assembly) and the complete Y chromosome, was used in this study to closely compare the H4K16 acetylation pattern between Jarid1c and Jarid1d present on the same array. Analysis was done using the manufacturer software.Supporting Information
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Using primers designed to test three Jarid1c sites (Supplementary Table S1). Enrichment for each histone mark was normalized against the input (5 of the amount of chromatin used in each antibody-mediated selection). As a negative control, instead of histone antibodies, normal rabbit serum was incubated with chromatin samples which resulted in barely detectable enrichment. Histone modifications on