Evidence map›Paper›PMID 23530048›Full record

ArticleThe Journal of biological chemistry2013

A prototypic lysine methyltransferase 4 from archaea with degenerate sequence specificity methylates chromatin proteins Sul7d and Cren7 in different patterns.

Yanling Niu, Yisui Xia, Sishuo Wang, Jiani Li, Caoyuan Niu, Xiao Li, Yuehui Zhao, Huiyang Xiong, Zhen Li, Huiqiang Lou and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Protein methylation in mitochondria.The Journal of biological chemistry · 2022
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  14. dbHiMo: a web-based epigenomics platform for histone-modifying enzymes.Database : the journal of biological databases and curation · 2015
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4 · The record

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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

11 authors at 2 institutions in 2 countries.

Yanling NiuState Key Laboratory of Agro-Biotechnology and Ministry of Agriculture Key Laboratory of Soil Microbiology, College of Biological Sciences, China Agricultural University, Beijing 100193, China.
Yisui Xia
Sishuo Wang
Jiani Li
Caoyuan Niu
Xiao Li
Yuehui Zhao
Huiyang Xiong
Zhen Li
Huiqiang Lou
Qinhong Cao
University of Minnesota · USChina Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe origin of eukaryotic histone modification enzymes still remains obscure.

resultsPrototypic KMT4/Dot1 from Archaea targets chromatin proteins (Sul7d and Cren7) and shows increased activity on Sul7d, but not Cren7, in the presence of DNA.

conclusionPromiscuous aKMT4 could be regulated by chromatin environment. SIGNIFICANCE: This study supports the prokaryotic origin model of eukaryotic histone methyltransferases and sheds light on chromatin dynamics in Archaea. Histone methylation is one of the major epigenetic modifications even in early diverging unicellular eukaryotes. We show that a widespread lysine methyltransferase from Archaea (aKMT4), bears striking structural and functional resemblance to the core of distantly related eukaryotic KMT4/Dot1. aKMT4 methylates a set of various proteins, including the chromatin proteins Sul7d and Cren7, and RNA exosome components. Csl4- and Rrp4-exosome complexes are methylated in different patterns. aKMT4 can self-methylate intramolecularly and compete with other proteins for the methyl group. Automethylation is inhibited by suitable substrates or DNA in a concentration-dependent manner. The automethylated enzyme shows relatively compromised activity. aKMT4-8A mutant with abrogated automethylation shows a more than 150% increase in methylation of substrates, suggesting a possible mechanism to regulate methyltransferase activity. More interestingly, methylation of Sul7d, but not Cren7, by aKMT4 is significantly enhanced by DNA. MS/MS and kinetic analysis further suggest that aKMT4 methylates Sul7d in the chromatin context. These data provide a clue to the possible regulation of aKMT4 activity by the local chromatin environment, albeit as a promiscuous enzyme required for extensive and variegated lysine methylation in Sulfolobus. This study supports the prokaryotic origin model of eukaryotic histone modification enzymes and sheds light on regulation of archaeal chromatin.

Indexed as

Protein Processing, Post-TranslationalAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionArchaeal ProteinsChromatinConserved SequenceDNA, ArchaealDNA-Binding ProteinsMethylationMolecular Sequence DataProtein MethyltransferasesSubstrate SpecificitySulfolobusArchaeal ProteinsChromatinDNA, ArchaealDNA-Binding ProteinsProtein MethyltransferasesArchaeaChromatin ModificationDNA-binding ProteinHistone MethylationProtein Methylation

Identifiers

PMID23530048
PMCPMC3650410
OpenAlexW2019702808

What OpenQuestion holds

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Read underepoch 390

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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.