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Life
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Structure, Activity, and Function of Protein Methyltransferases: 2nd Edition
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Structure, Activity, and Function of Protein Methyltransferases: 2nd Edition

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Proteins and Proteomics".

Deadline for manuscript submissions: 27 February 2026 | Viewed by 900

Special Issue Editors

Prof. Dr. Albert Jeltsch

E-Mail Website
Guest Editor
Institute of Biochemistry and Technical Biochemistry, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany
Interests: DNA methyltransferases; DNA methylation; protein methyltransferases; protein methylation; reading domains; molecular epigenetics; synthetic biology; molecular enzymology
Special Issues, Collections and Topics in MDPI journals
Dr. Arunkumar Dhayalan

E-Mail Website
Guest Editor
Department of Biotechnology, Pondicherry University, Puducherry 605014, India
Interests: protein arginine methyltransferases; histone arginine methylation; reader proteins; DEAD box family of RNA helicases
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Volume 2 of the highly successful Life Special Issue entitled "Structure, Activity, and Function of Protein Methyltransferases” (originally published in 2021, https://www.mdpi.com/journal/life/special_issues/protein_methyltransferases) will collect additional reviews, all written by leading experts in the field, about individual Protein methyltransferases and the specific biological roles of individual Protein methyltransferases in biological processes such as cancer, chromatin regulation, immune modulation, neurobiology and development. The scope covers Protein lysine methyltransferases, Protein arginine methyltransferases, but also the less abundant Protein glutamine methyltransferases, Protein histidine methyltransferases and Protein N-terminal end methyltransferases. It encompasses reviews of particular enzymes, groups of related enzymes and reviews in the light of particular biological processes of individual enzymes or groups of enzymes. This will make this Special Issue a unique and very useful resource for researchers from the Protein methylation and Protein methyltransferase field.

We invite suggestions for manuscripts to be included in this Special Issue. Please contact the editors before preparing the manuscript for a pre-arrangement of the topic.

Prof. Dr. Albert Jeltsch
Dr. Arunkumar Dhayalan
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Life is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

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Published Papers (1 paper)

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Research

15 pages, 3801 KB  
Article
Mechanisms of Substrate Recognition by the Multispecific Protein Lysine Methyltransferase SETD6
by Gizem T. Ulu, Sara Weirich, Jana Kehl, Thyagarajan T. Chandrasekaran, Franziska Dorscht, Dan Levy and Albert Jeltsch
Life 2025, 15(10), 1578; https://doi.org/10.3390/life15101578 - 10 Oct 2025
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Abstract
The SETD6 protein lysine methyltransferase monomethylates specific lysine residues in a diverse set of substrates which contain the target lysine residue in a highly variable amino acid sequence context. To investigate the mechanism underlying this multispecificity, we analyzed SETD6 substrate recognition using AlphaFold [...] Read more.
The SETD6 protein lysine methyltransferase monomethylates specific lysine residues in a diverse set of substrates which contain the target lysine residue in a highly variable amino acid sequence context. To investigate the mechanism underlying this multispecificity, we analyzed SETD6 substrate recognition using AlphaFold 3 docking and peptide SPOT array methylation experiments. Structural modeling of the SETD6–E2F1 complex suggested that substrate binding alone is insufficient to restrict SETD6 activity to only one lysine residue, pointing to additional sequence readout at the target site. Methylation of mutational scanning peptide SPOT arrays derived from four different SETD6 substrates (E2F1 K117, H2A.Z K7, RELA K310, and H4 K12) revealed sequence preferences of SETD6 at positions −1, +2, and +3 relative to the target lysine. Notably, glycine or large aliphatic residues were favored at −1, isoleucine/valine at +2, and lysine at +3. These preferences, however, were sequence context dependent and variably exploited among different substrates, indicating conformational variability of the enzyme–substrate interface. Mutation of SETD6 residue L260, which forms a contact with the +2 site in the available SETD6-RELA structure, further demonstrated substrate-specific differences in recognition at the +2/+3 sites. Together, these findings reveal a versatile mode of peptide recognition in which the readout of each substrate position depends on the overall substrate peptide sequence. These findings can explain the multispecificity of SETD6 and similar mechanisms may underlie substrate selection in other protein methyltransferases. Full article
(This article belongs to the Special Issue Structure, Activity, and Function of Protein Methyltransferases: 2nd Edition)
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