التفاصيل البيبلوغرافية
| العنوان: |
Effects of Oncohistone Mutations and PTM Crosstalk on the N‑Terminal Acetylation Activities of NatD |
| المؤلفون: |
Yi-Hsun Ho (6107591), Rong Huang (298496) |
| سنة النشر: |
2022 |
| المجموعة: |
Smithsonian Institution: Digital Repository |
| مصطلحات موضوعية: |
Biophysics, Biochemistry, Microbiology, Genetics, Molecular Biology, Plant Biology, Virology, Biological Sciences not elsewhere classified, Physical Sciences not elsewhere classified, local chemical environment, highlighting different avenues, abundant modification detected, terminal sgrgk sequence, h4 ser1 phosphorylation, sgrg suppressed natd, ptms affect natd, terminal acetyltransferase, histone h4, natd activity, work reveals, translational modifications, studies indicate, oncohistone mutations, natd acetylation, naa40 ), mediated pathway, marginal effect |
| الوصف: |
Acetylation at the α-N-terminus (Nα) is the most abundant modification detected on histone H4 and H2A, which is catalyzed by N-terminal acetyltransferase D (NatD or NAA40). Histone H4 and H2A contain an identical N-terminal SGRGK sequence that is enriched with post-translational modifications (PTMs) and frequently occurred oncogenic mutations known as “oncohistone” mutations. However, there is a lack of information on how oncohistone mutations and other PTMs affect NatD-catalyzed acetylation. Herein, we determined how the local chemical environment on the N-terminal SGRGK sequence impacts NatD-catalyzed Nα-acetylation on histone H4/H2A. Our studies indicate that all oncohistone mutations at SGRG suppressed NatD-catalyzed acetylation. Meanwhile, H4 Ser1 phosphorylation and Arg3 methylation negatively impact the NatD-mediated acetylation, but the Lys5 acetylation only has a marginal effect. This work reveals the impacts of oncohistone mutations on NatD activity and unravels the crosstalk between NatD and PTMs, implying potential regulatory mechanism of NatD and highlighting different avenues to interrogate the NatD-mediated pathway in the future. |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
unknown |
| العلاقة: |
https://figshare.com/articles/journal_contribution/Effects_of_Oncohistone_Mutations_and_PTM_Crosstalk_on_the_N_Terminal_Acetylation_Activities_of_NatD/18737276Test |
| DOI: |
10.1021/acschembio.1c00840.s001 |
| الإتاحة: |
https://doi.org/10.1021/acschembio.1c00840.s001Test |
| حقوق: |
CC BY-NC 4.0 |
| رقم الانضمام: |
edsbas.FD2B596C |
| قاعدة البيانات: |
BASE |
