Cargando…
Substrate Scope for Human Histone Lysine Acetyltransferase KAT8
Biomedically important histone lysine acetyltransferase KAT8 catalyses the acetyl coenzyme A-dependent acetylation of lysine on histone and other proteins. Here, we explore the ability of human KAT8 to catalyse the acetylation of histone H4 peptides possessing lysine and its analogues at position 16...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7830570/ https://www.ncbi.nlm.nih.gov/pubmed/33467728 http://dx.doi.org/10.3390/ijms22020846 |
_version_ | 1783641446765559808 |
---|---|
author | Proietti, Giordano Wang, Yali Punzo, Chiara Mecinović, Jasmin |
author_facet | Proietti, Giordano Wang, Yali Punzo, Chiara Mecinović, Jasmin |
author_sort | Proietti, Giordano |
collection | PubMed |
description | Biomedically important histone lysine acetyltransferase KAT8 catalyses the acetyl coenzyme A-dependent acetylation of lysine on histone and other proteins. Here, we explore the ability of human KAT8 to catalyse the acetylation of histone H4 peptides possessing lysine and its analogues at position 16 (H4K16). Our synthetic and enzymatic studies on chemically and structurally diverse lysine mimics demonstrate that KAT8 also has a capacity to acetylate selected lysine analogues that possess subtle changes on the side chain and main chain. Overall, this work highlights that KAT8 has a broader substrate scope beyond natural lysine, and contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase (KAT) family. |
format | Online Article Text |
id | pubmed-7830570 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-78305702021-01-26 Substrate Scope for Human Histone Lysine Acetyltransferase KAT8 Proietti, Giordano Wang, Yali Punzo, Chiara Mecinović, Jasmin Int J Mol Sci Article Biomedically important histone lysine acetyltransferase KAT8 catalyses the acetyl coenzyme A-dependent acetylation of lysine on histone and other proteins. Here, we explore the ability of human KAT8 to catalyse the acetylation of histone H4 peptides possessing lysine and its analogues at position 16 (H4K16). Our synthetic and enzymatic studies on chemically and structurally diverse lysine mimics demonstrate that KAT8 also has a capacity to acetylate selected lysine analogues that possess subtle changes on the side chain and main chain. Overall, this work highlights that KAT8 has a broader substrate scope beyond natural lysine, and contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase (KAT) family. MDPI 2021-01-15 /pmc/articles/PMC7830570/ /pubmed/33467728 http://dx.doi.org/10.3390/ijms22020846 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Proietti, Giordano Wang, Yali Punzo, Chiara Mecinović, Jasmin Substrate Scope for Human Histone Lysine Acetyltransferase KAT8 |
title | Substrate Scope for Human Histone Lysine Acetyltransferase KAT8 |
title_full | Substrate Scope for Human Histone Lysine Acetyltransferase KAT8 |
title_fullStr | Substrate Scope for Human Histone Lysine Acetyltransferase KAT8 |
title_full_unstemmed | Substrate Scope for Human Histone Lysine Acetyltransferase KAT8 |
title_short | Substrate Scope for Human Histone Lysine Acetyltransferase KAT8 |
title_sort | substrate scope for human histone lysine acetyltransferase kat8 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7830570/ https://www.ncbi.nlm.nih.gov/pubmed/33467728 http://dx.doi.org/10.3390/ijms22020846 |
work_keys_str_mv | AT proiettigiordano substratescopeforhumanhistonelysineacetyltransferasekat8 AT wangyali substratescopeforhumanhistonelysineacetyltransferasekat8 AT punzochiara substratescopeforhumanhistonelysineacetyltransferasekat8 AT mecinovicjasmin substratescopeforhumanhistonelysineacetyltransferasekat8 |