Protein lysine methylation by seven-β-strand methyltransferases
(2016) In The Biochemical journal 473(14). p.1995-2009- Abstract
Methylation of biomolecules is a frequent biochemical reaction within the cell, and a plethora of highly specific methyltransferases (MTases) catalyse the transfer of a methyl group from S-adenosylmethionine (AdoMet) to various substrates. The posttranslational methylation of lysine residues, catalysed by numerous lysine (K)-specific protein MTases (KMTs), is a very common and important protein modification, which recently has been subject to intense studies, particularly in the case of histone proteins. The majority of KMTs belong to a class of MTases that share a defining 'SET domain', and these enzymes mostly target lysines in the flexible tails of histones. However, the so-called seven-β-strand (7BS) MTases, characterized by a... (More)
Methylation of biomolecules is a frequent biochemical reaction within the cell, and a plethora of highly specific methyltransferases (MTases) catalyse the transfer of a methyl group from S-adenosylmethionine (AdoMet) to various substrates. The posttranslational methylation of lysine residues, catalysed by numerous lysine (K)-specific protein MTases (KMTs), is a very common and important protein modification, which recently has been subject to intense studies, particularly in the case of histone proteins. The majority of KMTs belong to a class of MTases that share a defining 'SET domain', and these enzymes mostly target lysines in the flexible tails of histones. However, the so-called seven-β-strand (7BS) MTases, characterized by a twisted beta-sheet structure and certain conserved sequence motifs, represent the largest MTase class, and these enzymes methylate a wide range of substrates, including small metabolites, lipids, nucleic acids and proteins. Until recently, the histone-specific Dot1/DOT1L was the only identified eukaryotic 7BS KMT. However, a number of novel 7BS KMTs have now been discovered, and, in particular, several recently characterized human and yeast members of MTase family 16 (MTF16) have been found to methylate lysines in non-histone proteins. Here, we review the status and recent progress on the 7BS KMTs, and discuss these enzymes at the levels of sequence/structure, catalytic mechanism, substrate recognition and biological significance.
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- author
- Falnes, Pål Ø ; Jakobsson, Magnus E LU ; Davydova, Erna ; Ho, Angela and Małecki, Jędrzej
- publishing date
- 2016-07-15
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Animals, Histone-Lysine N-Methyltransferase, Humans, Lysine/metabolism, Methylation, Methyltransferases/metabolism, Protein Processing, Post-Translational, Substrate Specificity
- in
- The Biochemical journal
- volume
- 473
- issue
- 14
- pages
- 15 pages
- publisher
- Portland Press
- external identifiers
-
- pmid:27407169
- scopus:85009384604
- ISSN
- 0264-6021
- DOI
- 10.1042/BCJ20160117
- language
- English
- LU publication?
- no
- additional info
- © 2016 The Author(s). published by Portland Press Limited on behalf of the Biochemical Society.
- id
- 5cfbd217-6ecc-42c2-9d38-b73d7ba67508
- date added to LUP
- 2020-01-13 08:54:36
- date last changed
- 2024-06-27 12:06:26
@article{5cfbd217-6ecc-42c2-9d38-b73d7ba67508,
abstract = {{<p>Methylation of biomolecules is a frequent biochemical reaction within the cell, and a plethora of highly specific methyltransferases (MTases) catalyse the transfer of a methyl group from S-adenosylmethionine (AdoMet) to various substrates. The posttranslational methylation of lysine residues, catalysed by numerous lysine (K)-specific protein MTases (KMTs), is a very common and important protein modification, which recently has been subject to intense studies, particularly in the case of histone proteins. The majority of KMTs belong to a class of MTases that share a defining 'SET domain', and these enzymes mostly target lysines in the flexible tails of histones. However, the so-called seven-β-strand (7BS) MTases, characterized by a twisted beta-sheet structure and certain conserved sequence motifs, represent the largest MTase class, and these enzymes methylate a wide range of substrates, including small metabolites, lipids, nucleic acids and proteins. Until recently, the histone-specific Dot1/DOT1L was the only identified eukaryotic 7BS KMT. However, a number of novel 7BS KMTs have now been discovered, and, in particular, several recently characterized human and yeast members of MTase family 16 (MTF16) have been found to methylate lysines in non-histone proteins. Here, we review the status and recent progress on the 7BS KMTs, and discuss these enzymes at the levels of sequence/structure, catalytic mechanism, substrate recognition and biological significance.</p>}},
author = {{Falnes, Pål Ø and Jakobsson, Magnus E and Davydova, Erna and Ho, Angela and Małecki, Jędrzej}},
issn = {{0264-6021}},
keywords = {{Animals; Histone-Lysine N-Methyltransferase; Humans; Lysine/metabolism; Methylation; Methyltransferases/metabolism; Protein Processing, Post-Translational; Substrate Specificity}},
language = {{eng}},
month = {{07}},
number = {{14}},
pages = {{1995--2009}},
publisher = {{Portland Press}},
series = {{The Biochemical journal}},
title = {{Protein lysine methylation by seven-β-strand methyltransferases}},
url = {{http://dx.doi.org/10.1042/BCJ20160117}},
doi = {{10.1042/BCJ20160117}},
volume = {{473}},
year = {{2016}},
}