TgKDAC4: A Unique Deacetylase of Toxoplasma’s Apicoplast

Author:

Fragoso Mariana Sayuri Ishikawa1,de Siqueira Caroline Moraes1,Vitorino Francisca Nathália Luna2ORCID,Vieira Alexandre Zanatta1ORCID,Martins-Duarte Érica Santos3ORCID,Faoro Helisson1,da Cunha Júlia Pinheiro Chagas2,Ávila Andréa Rodrigues1ORCID,Nardelli Sheila Cristina1ORCID

Affiliation:

1. Instituto Carlos Chagas, Fundação Oswaldo Cruz, Curitiba 81350-010, Brazil

2. Special Laboratory of Cell Cycle, Center of Toxins, Immune Response and Cell Signalling (CeTICS), Instituto Butantan, São Paulo 05503-900, Brazil

3. Department of Parasitology, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte 31270-901, Brazil

Abstract

Toxoplasma gondii is an obligate intracellular parasite of the phylum Apicomplexa and causes toxoplasmosis infections, a disease that affects a quarter of the world’s population and has no effective cure. Epigenetic regulation is one of the mechanisms controlling gene expression and plays an essential role in all organisms. Lysine deacetylases (KDACs) act as epigenetic regulators affecting gene silencing in many eukaryotes. Here, we focus on TgKDAC4, an enzyme unique to apicomplexan parasites, and a class IV KDAC, the least-studied class of deacetylases so far. This enzyme shares only a portion of the specific KDAC domain with other organisms. Phylogenetic analysis from the TgKDAC4 domain shows a putative prokaryotic origin. Surprisingly, TgKDAC4 is located in the apicoplast, making it the only KDAC found in this organelle to date. Transmission electron microscopy assays confirmed the presence of TgKDAC4 in the periphery of the apicoplast. We identified possible targets or/and partners of TgKDAC4 by immunoprecipitation assays followed by mass spectrometry analysis, including TgCPN60 and TgGAPDH2, both located at the apicoplast and containing acetylation sites. Understanding how the protein works could provide new insights into the metabolism of the apicoplast, an essential organelle for parasite survival.

Funder

FIOCRUZ

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Fundação Araucária/CNPq

Fundação de Amparo a Pesquisa do Estado de São Paulo

Publisher

MDPI AG

Subject

Virology,Microbiology (medical),Microbiology

Reference83 articles.

1. Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions;Choudhary;Science,2009

2. The Presence of Acetyl Groups in Histones;Philllips;Biochem. J.,1963

3. The Protein Acetylome and the Regulation of Metabolism;Xing;Trends Plant Sci.,2012

4. Acetylation and Methylation Of Histones and Their Possible Role in the Regulation of RNA Synthesis;Allfrey;Biochemistry,1964

5. Functions and Mechanisms of Non-Histone Protein Acetylation;Narita;Nat. Rev. Mol. Cell Biol.,2019

Cited by 1 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3