Histone H3 and H3.3 variants in the protozoan pathogens Plasmodium falciparum and Toxoplasma gondii

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Histones constitute the fundamental component of chromatin and participate in the regulation of gene expression by virtue of covalent modifications to their N-terminal domains. The discovery that histone-modifying enzymes are targeted by the antiprotozoal agent apicidin has prompted further investigation of gene expression regulation in protozoan parasites; consequently, several chromatin remodeling homologues with unusual features have been isolated. To facilitate investigation of these chromatin remodeling homologues using parasite-specific substrates, we sought to clone and characterize histone H3 from two medically significant pathogens in the phylum Apicomplexa: Plasmodium falciparum (malaria) and Toxoplasma gondii (opportunistic pathogen of immunocompromised individuals). Like most eukaryotic organisms, these parasites each contain at least two histone H3 variants, termed H3 and H3.3. Sequence analysis reveals the Apicomplexan H3 proteins harbor novel and rare features. Expression and purification of recombinant H3 variants will provide species-specific substrate for the analysis of the histone-modifying machinery of these parasites.

Original languageEnglish
Pages (from-to)227-231
Number of pages5
JournalDNA Sequence - Journal of DNA Sequencing and Mapping
Volume14
Issue number3
DOIs
StatePublished - Jun 2003

Fingerprint

Toxoplasma
Pathogens
Plasmodium falciparum
Histones
Parasites
Chromatin
Chromatin Assembly and Disassembly
Gene Expression Regulation
Gene expression regulation
Antiprotozoal Agents
Apicomplexa
Falciparum Malaria
Substrates
Ports and harbors
Gene expression
Machinery
Purification
Sequence Analysis
Clone Cells
Enzymes

Keywords

  • Apicomplexan
  • Chromatin
  • Nucleosome
  • Parasite
  • Transcription

ASJC Scopus subject areas

  • Genetics
  • Biochemistry
  • Endocrinology
  • Molecular Biology

Cite this

@article{4e8db357b1994af6aa0badadc82fd0bf,
title = "Histone H3 and H3.3 variants in the protozoan pathogens Plasmodium falciparum and Toxoplasma gondii",
abstract = "Histones constitute the fundamental component of chromatin and participate in the regulation of gene expression by virtue of covalent modifications to their N-terminal domains. The discovery that histone-modifying enzymes are targeted by the antiprotozoal agent apicidin has prompted further investigation of gene expression regulation in protozoan parasites; consequently, several chromatin remodeling homologues with unusual features have been isolated. To facilitate investigation of these chromatin remodeling homologues using parasite-specific substrates, we sought to clone and characterize histone H3 from two medically significant pathogens in the phylum Apicomplexa: Plasmodium falciparum (malaria) and Toxoplasma gondii (opportunistic pathogen of immunocompromised individuals). Like most eukaryotic organisms, these parasites each contain at least two histone H3 variants, termed H3 and H3.3. Sequence analysis reveals the Apicomplexan H3 proteins harbor novel and rare features. Expression and purification of recombinant H3 variants will provide species-specific substrate for the analysis of the histone-modifying machinery of these parasites.",
keywords = "Apicomplexan, Chromatin, Nucleosome, Parasite, Transcription",
author = "William Sullivan",
year = "2003",
month = "6",
doi = "10.1080/1042517031000089496",
language = "English",
volume = "14",
pages = "227--231",
journal = "DNA Sequence - Journal of DNA Sequencing and Mapping",
issn = "1940-1736",
publisher = "Informa Healthcare",
number = "3",

}

TY - JOUR

T1 - Histone H3 and H3.3 variants in the protozoan pathogens Plasmodium falciparum and Toxoplasma gondii

AU - Sullivan, William

PY - 2003/6

Y1 - 2003/6

N2 - Histones constitute the fundamental component of chromatin and participate in the regulation of gene expression by virtue of covalent modifications to their N-terminal domains. The discovery that histone-modifying enzymes are targeted by the antiprotozoal agent apicidin has prompted further investigation of gene expression regulation in protozoan parasites; consequently, several chromatin remodeling homologues with unusual features have been isolated. To facilitate investigation of these chromatin remodeling homologues using parasite-specific substrates, we sought to clone and characterize histone H3 from two medically significant pathogens in the phylum Apicomplexa: Plasmodium falciparum (malaria) and Toxoplasma gondii (opportunistic pathogen of immunocompromised individuals). Like most eukaryotic organisms, these parasites each contain at least two histone H3 variants, termed H3 and H3.3. Sequence analysis reveals the Apicomplexan H3 proteins harbor novel and rare features. Expression and purification of recombinant H3 variants will provide species-specific substrate for the analysis of the histone-modifying machinery of these parasites.

AB - Histones constitute the fundamental component of chromatin and participate in the regulation of gene expression by virtue of covalent modifications to their N-terminal domains. The discovery that histone-modifying enzymes are targeted by the antiprotozoal agent apicidin has prompted further investigation of gene expression regulation in protozoan parasites; consequently, several chromatin remodeling homologues with unusual features have been isolated. To facilitate investigation of these chromatin remodeling homologues using parasite-specific substrates, we sought to clone and characterize histone H3 from two medically significant pathogens in the phylum Apicomplexa: Plasmodium falciparum (malaria) and Toxoplasma gondii (opportunistic pathogen of immunocompromised individuals). Like most eukaryotic organisms, these parasites each contain at least two histone H3 variants, termed H3 and H3.3. Sequence analysis reveals the Apicomplexan H3 proteins harbor novel and rare features. Expression and purification of recombinant H3 variants will provide species-specific substrate for the analysis of the histone-modifying machinery of these parasites.

KW - Apicomplexan

KW - Chromatin

KW - Nucleosome

KW - Parasite

KW - Transcription

UR - http://www.scopus.com/inward/record.url?scp=0038445820&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0038445820&partnerID=8YFLogxK

U2 - 10.1080/1042517031000089496

DO - 10.1080/1042517031000089496

M3 - Article

VL - 14

SP - 227

EP - 231

JO - DNA Sequence - Journal of DNA Sequencing and Mapping

JF - DNA Sequence - Journal of DNA Sequencing and Mapping

SN - 1940-1736

IS - 3

ER -