인문학
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자연과학
공학
의약학
농수해양학
예술체육학
복합학
DBpia AI
AI 에이전트
AI 아이디어
AI 리더
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Citeasy
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지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록·키워드
Members of the Jumonji C (JmjC) subfamily of non-heme Fe(ii) and 2-oxoglutarate (2OG) dependent <i>N</i> <sup>ε</sup>-lysine demethylases have established roles in catalysing demethylation of <i>N</i> <sup>ε</sup>-methylated lysine residues in core histones; their roles in accepting linker H1 histones as substrates have been less well explored. We report studies on the H1 substrate specificity of human JmjC lysine demethylases (KDMs), specifically KDM3A-C, KDM4A, KDM4D, KDM4E, KDM5D, and KDM6B, for mono-, di- and trimethylated <i>N</i> <sup>ε</sup>-lysine residues in peptide fragments of the N-terminal tail of human linker histone H1 isoforms (H1.2, H1.3, H1.4 and H1.5). The KDM4s, but not the other tested JmjC KDMs, catalysed demethylation of tri- and dimethylated H1 peptide isoforms with activities: KDM4E > KDM4D > KDM4A. The order of substrate preference for KDM4E was H1.2K26me3 > H1.5K26me3 ≈ H1.3K24me3 > H1.2K25me3 ≈ H1.4K25me3. For KDM4D, the most efficient tested substrate was H1.5K26me3. Among the dimethylated H1 peptide isoforms, H1.3K24me2 appeared to be the most efficient KDM4E substrate, with comparable activity to the core histone H3K9me2 substrate. The results demonstrate that JmjC KDM4s can accept the N-terminal H1 tails as substrates, further highlighting the potential for flexibility in substrate and product selectivity of the JmjC KDMs, in particular, within the KDM4 subfamily. Molecular and cellular investigations on JmjC KDM-catalysed H1 demethylation are of molecular and biomedical interest.
인공지능 문자 인식 모델을 통해 추출된 텍스트로, 일부 오타나 오류가 포함될 수 있으나 지속적으로 개선 중입니다.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
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