{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe provided abstract (PMID:"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "does not address the function of MIR548AS. Instead, it details how JMJD5 and JMJD7 act as histone tail–clipping proteases. These enzymes specifically recognize and cleave histone tails at sites adjacent to methylated arginine residues, using a two‐step proteolytic mechanism that involves both endopeptidase and aminopeptidase activities. This process generates “tailless” nucleosomes that facilitate the transition of paused RNA polymerase II into productive transcription elongation. Structural studies reveal that JMJD5 contains a Tudor domain–like binding pocket for the methylated arginine side chain and features a nearby glutamine that may be key to a unique imidic acid–mediated catalytic mechanism. Notably, substrate specificity is finely tuned as JMJD5 and JMJD7 show differential binding in the presence of additional lysine modifications, underscoring a nuanced regulation of chromatin dynamics."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Haolin Liu, Chao Wang, Schuyler Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Specific Recognition of Arginine Methylated Histone Tails by JMJD5 and JMJD7."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-018-21432-8"}], "href": "https://doi.org/10.1038/s41598-018-21432-8"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29459673"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29459673"}]}]}]}