Cargando…

Protein acetylation: an important mechanism in actinobacteria

This is a commentary on the research article by Lu et al. recently published in Bioscience Reports. The GCN5-like acetyltransferases with amino acid-binding (ACT)-GCN5-related N-acetyltransferase (GNAT) domain organization have been identified in actinobacteria by Lu et al. (2017). The ACT domain is...

Descripción completa

Detalles Bibliográficos
Autores principales: Zhang, Huaidong, Xu, Ximing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5861322/
https://www.ncbi.nlm.nih.gov/pubmed/29301868
http://dx.doi.org/10.1042/BSR20170851
_version_ 1783308073248489472
author Zhang, Huaidong
Xu, Ximing
author_facet Zhang, Huaidong
Xu, Ximing
author_sort Zhang, Huaidong
collection PubMed
description This is a commentary on the research article by Lu et al. recently published in Bioscience Reports. The GCN5-like acetyltransferases with amino acid-binding (ACT)-GCN5-related N-acetyltransferase (GNAT) domain organization have been identified in actinobacteria by Lu et al. (2017). The ACT domain is fused to the GNAT domain, conferring amino acid-induced allosteric regulation to these protein acetyltransferases (Pat) (amino acid sensing acetyltransferase (AAPatA)). Members of the AAPatA family share similar secondary structure and are divided into two groups based on the allosteric ligands of the ACT domain: the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former are mainly found in Streptomyces; the latter are distributed in other actinobacteria. The authors investigated the effect of Asn and Cys on the acetylation activity of Sven_0867 (SvePatA, from Streptomyces venezuelae DSM 40230) and Amir_5672 (AmiPatA, from Actinosynnema mirum strain DSM 43827), respectively, as well as the relationship between the structure and function of these enzymes. Research history and progress on acetyltransferases and lysine acetylation of proteins were discussed. The activity of PatA and acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in actinobacteria.
format Online
Article
Text
id pubmed-5861322
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher Portland Press Ltd.
record_format MEDLINE/PubMed
spelling pubmed-58613222018-04-05 Protein acetylation: an important mechanism in actinobacteria Zhang, Huaidong Xu, Ximing Biosci Rep Commentaries This is a commentary on the research article by Lu et al. recently published in Bioscience Reports. The GCN5-like acetyltransferases with amino acid-binding (ACT)-GCN5-related N-acetyltransferase (GNAT) domain organization have been identified in actinobacteria by Lu et al. (2017). The ACT domain is fused to the GNAT domain, conferring amino acid-induced allosteric regulation to these protein acetyltransferases (Pat) (amino acid sensing acetyltransferase (AAPatA)). Members of the AAPatA family share similar secondary structure and are divided into two groups based on the allosteric ligands of the ACT domain: the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former are mainly found in Streptomyces; the latter are distributed in other actinobacteria. The authors investigated the effect of Asn and Cys on the acetylation activity of Sven_0867 (SvePatA, from Streptomyces venezuelae DSM 40230) and Amir_5672 (AmiPatA, from Actinosynnema mirum strain DSM 43827), respectively, as well as the relationship between the structure and function of these enzymes. Research history and progress on acetyltransferases and lysine acetylation of proteins were discussed. The activity of PatA and acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in actinobacteria. Portland Press Ltd. 2018-03-21 /pmc/articles/PMC5861322/ /pubmed/29301868 http://dx.doi.org/10.1042/BSR20170851 Text en © 2018 The Author(s). http://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (http://creativecommons.org/licenses/by/4.0/) .
spellingShingle Commentaries
Zhang, Huaidong
Xu, Ximing
Protein acetylation: an important mechanism in actinobacteria
title Protein acetylation: an important mechanism in actinobacteria
title_full Protein acetylation: an important mechanism in actinobacteria
title_fullStr Protein acetylation: an important mechanism in actinobacteria
title_full_unstemmed Protein acetylation: an important mechanism in actinobacteria
title_short Protein acetylation: an important mechanism in actinobacteria
title_sort protein acetylation: an important mechanism in actinobacteria
topic Commentaries
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5861322/
https://www.ncbi.nlm.nih.gov/pubmed/29301868
http://dx.doi.org/10.1042/BSR20170851
work_keys_str_mv AT zhanghuaidong proteinacetylationanimportantmechanisminactinobacteria
AT xuximing proteinacetylationanimportantmechanisminactinobacteria