Evidence map›Paper›PMID 33839154›Full record

ArticleThe Journal of biological chemistry

Dynamic association of the H3K64 trimethylation mark with genes encoding exported proteins in Plasmodium falciparum.

C A Jabeena, Gayathri Govindaraju, Mukul Rawat, Soundhararajan Gopi, Devadathan Valiyamangalath Sethumadhavan, Abdul Jaleel, Dhakshmi Sasankan, Krishanpal Karmodiya, Arumugam Rajavelu

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 1 country.

C A JabeenaPathogen Biology Group, Rajiv Gandhi Centre for Biotechnology (RGCB), Thiruvananthapuram, Kerala, India; Manipal Academy of Higher Education (MAHE), Manipal, Karnataka, India.
Gayathri GovindarajuPathogen Biology Group, Rajiv Gandhi Centre for Biotechnology (RGCB), Thiruvananthapuram, Kerala, India; Manipal Academy of Higher Education (MAHE), Manipal, Karnataka, India.
Mukul RawatDepartment of Biology, Indian Institute of Science Education and Research, Pune, Maharashtra, India.
Soundhararajan GopiDepartment of Biotechnology, Bhupat & Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, India.
Devadathan Valiyamangalath SethumadhavanPathogen Biology Group, Rajiv Gandhi Centre for Biotechnology (RGCB), Thiruvananthapuram, Kerala, India; Manipal Academy of Higher Education (MAHE), Manipal, Karnataka, India.
Abdul JaleelCardiovascular Disease Biology, Rajiv Gandhi Centre for Biotechnology (RGCB), Thiruvananthapuram, Kerala, India.
Dhakshmi SasankanPathogen Biology Group, Rajiv Gandhi Centre for Biotechnology (RGCB), Thiruvananthapuram, Kerala, India.
Krishanpal KarmodiyaDepartment of Biology, Indian Institute of Science Education and Research, Pune, Maharashtra, India.
Arumugam RajaveluPathogen Biology Group, Rajiv Gandhi Centre for Biotechnology (RGCB), Thiruvananthapuram, Kerala, India. Electronic address: arajavelu@rgcb.res.in.
Manipal Academy of Higher Education · INRajiv Gandhi Centre for Biotechnology · INIndian Institute of Science Education and Research Pune · INIndian Institute of Technology Madras · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epigenetic modifications have emerged as critical regulators of virulence genes and stage-specific gene expression in Plasmodium falciparum. However, the specific roles of histone core epigenetic modifications in regulating the stage-specific gene expression are not well understood. In this study, we report an unconventional trimethylation at lysine 64 on histone 3 (H3K64me3) and characterize its functional relevance in P. falciparum. We show that PfSET4 and PfSET5 proteins of P. falciparum methylate H3K64 and that they prefer the nucleosome as a substrate over free histone 3 proteins. Structural analysis of PfSET5 revealed that it interacts with the nucleosome as a dimer. The H3K64me3 mark is dynamic, being enriched in the ring and trophozoite stages and drastically reduced in the schizont stages. Stage-specific global chromatin immunoprecipitation -sequencing analysis of the H3K64me3 mark revealed the selective enrichment of this methyl mark on the genes of exported family proteins in the ring and trophozoite stages and a significant reduction of the same in the schizont stages. Collectively, our data identify a novel epigenetic mark that is associated with the subset of genes encoding for exported proteins, which may regulate their expression in different stages of P. falciparum.

Indexed as

Histone CodeDNA MethylationErythrocytesHistonesHumansLysineMalaria, FalciparumNucleosomesPlasmodium falciparumProtozoan ProteinsHistonesLysineNucleosomesProtozoan ProteinsEpigeneticsexported family proteinshistone methylationmalarianucleosome

Identifiers

PMID33839154
PMCPMC8095176
OpenAlexW3151460478

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.