γ-Thialysine versus Lysine

An Insight into the Epigenetic Methylation of Histones

Abbas H. K. Al Temimi, Renate van der Wekken-de Bruijne, Giordano Proietti, Hong Guo, Ping Qian, Jasmin Mecinović

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Biomedicinally important histone lysine methyltransferases (KMTs) transfer a methyl group from S-adenosylmethionine to lysine residues in histones and other proteins. Here, we report comparative studies on epigenetic methylation of lysine and γ-thialysine, the simplest cysteine-derived lysine analog, which can be introduced to histone peptides and histone proteins via site-specific bioconjugation-based cysteine alkylation. Enzyme assays and computational studies demonstrate that human KMTs catalyze efficient methylation of histones that possess γ-thialysine. This work provides a molecular basis for the application of γ-thialysine for biomolecular studies of intact histones and the nucleosome assembly.
OriginalsprogEngelsk
TidsskriftBioconjugate Chemistry
Vol/bind30
Udgave nummer6
Sider (fra-til)1798-1804
ISSN1043-1802
DOI
StatusUdgivet - 19. jun. 2019

Fingeraftryk

Methylation
Epigenomics
Histones
Lysine
Proteins
Alkylation
Peptides
Assays
Enzymes
Cysteine
Histone-Lysine N-Methyltransferase
S-Adenosylmethionine
Nucleosomes
S-2-aminoethyl cysteine

Citer dette

Temimi, Abbas H. K. Al ; Bruijne, Renate van der Wekken-de ; Proietti, Giordano ; Guo, Hong ; Qian, Ping ; Mecinović, Jasmin. / γ-Thialysine versus Lysine : An Insight into the Epigenetic Methylation of Histones. I: Bioconjugate Chemistry. 2019 ; Bind 30, Nr. 6. s. 1798-1804.
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abstract = "Biomedicinally important histone lysine methyltransferases (KMTs) transfer a methyl group from S-adenosylmethionine to lysine residues in histones and other proteins. Here, we report comparative studies on epigenetic methylation of lysine and γ-thialysine, the simplest cysteine-derived lysine analog, which can be introduced to histone peptides and histone proteins via site-specific bioconjugation-based cysteine alkylation. Enzyme assays and computational studies demonstrate that human KMTs catalyze efficient methylation of histones that possess γ-thialysine. This work provides a molecular basis for the application of γ-thialysine for biomolecular studies of intact histones and the nucleosome assembly.",
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γ-Thialysine versus Lysine : An Insight into the Epigenetic Methylation of Histones. / Temimi, Abbas H. K. Al; Bruijne, Renate van der Wekken-de; Proietti, Giordano; Guo, Hong; Qian, Ping; Mecinović, Jasmin.

I: Bioconjugate Chemistry, Bind 30, Nr. 6, 19.06.2019, s. 1798-1804.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - γ-Thialysine versus Lysine

T2 - An Insight into the Epigenetic Methylation of Histones

AU - Temimi, Abbas H. K. Al

AU - Bruijne, Renate van der Wekken-de

AU - Proietti, Giordano

AU - Guo, Hong

AU - Qian, Ping

AU - Mecinović, Jasmin

PY - 2019/6/19

Y1 - 2019/6/19

N2 - Biomedicinally important histone lysine methyltransferases (KMTs) transfer a methyl group from S-adenosylmethionine to lysine residues in histones and other proteins. Here, we report comparative studies on epigenetic methylation of lysine and γ-thialysine, the simplest cysteine-derived lysine analog, which can be introduced to histone peptides and histone proteins via site-specific bioconjugation-based cysteine alkylation. Enzyme assays and computational studies demonstrate that human KMTs catalyze efficient methylation of histones that possess γ-thialysine. This work provides a molecular basis for the application of γ-thialysine for biomolecular studies of intact histones and the nucleosome assembly.

AB - Biomedicinally important histone lysine methyltransferases (KMTs) transfer a methyl group from S-adenosylmethionine to lysine residues in histones and other proteins. Here, we report comparative studies on epigenetic methylation of lysine and γ-thialysine, the simplest cysteine-derived lysine analog, which can be introduced to histone peptides and histone proteins via site-specific bioconjugation-based cysteine alkylation. Enzyme assays and computational studies demonstrate that human KMTs catalyze efficient methylation of histones that possess γ-thialysine. This work provides a molecular basis for the application of γ-thialysine for biomolecular studies of intact histones and the nucleosome assembly.

U2 - 10.1021/acs.bioconjchem.9b00313

DO - 10.1021/acs.bioconjchem.9b00313

M3 - Journal article

VL - 30

SP - 1798

EP - 1804

JO - Bioconjugate Chemistry

JF - Bioconjugate Chemistry

SN - 1043-1802

IS - 6

ER -