Enzymology and significance of protein histidine methylation
(2021) In The Journal of biological chemistry 297(4).- Abstract
Cells synthesize proteins using 20 standard amino acids and expand their biochemical repertoire through intricate enzyme-mediated post-translational modifications (PTMs). PTMs can either be static and represent protein editing events or be dynamically regulated as a part of a cellular response to specific stimuli. Protein histidine methylation (Hme) was an elusive PTM for over 5 decades and has only recently attracted considerable attention through discoveries concerning its enzymology, extent, and function. Here, we review the status of the Hme field and discuss the implications of Hme in physiological and cellular processes. We also review the experimental toolbox for analysis of Hme and discuss the strengths and weaknesses of... (More)
Cells synthesize proteins using 20 standard amino acids and expand their biochemical repertoire through intricate enzyme-mediated post-translational modifications (PTMs). PTMs can either be static and represent protein editing events or be dynamically regulated as a part of a cellular response to specific stimuli. Protein histidine methylation (Hme) was an elusive PTM for over 5 decades and has only recently attracted considerable attention through discoveries concerning its enzymology, extent, and function. Here, we review the status of the Hme field and discuss the implications of Hme in physiological and cellular processes. We also review the experimental toolbox for analysis of Hme and discuss the strengths and weaknesses of different experimental approaches. The findings discussed in this review demonstrate that Hme is widespread across cells and tissues and functionally regulates key cellular processes such as cytoskeletal dynamics and protein translation. Collectively, the findings discussed here showcase Hme as a regulator of key cellular functions and highlight the regulation of this modification as an emerging field of biological research.
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- author
- Jakobsson, Magnus E LU
- organization
- publishing date
- 2021-10
- type
- Contribution to journal
- publication status
- published
- subject
- in
- The Journal of biological chemistry
- volume
- 297
- issue
- 4
- article number
- 101130
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- scopus:85115418549
- pmid:34461099
- ISSN
- 1083-351X
- DOI
- 10.1016/j.jbc.2021.101130
- language
- English
- LU publication?
- yes
- additional info
- Copyright © 2021 The Author. Published by Elsevier Inc. All rights reserved.
- id
- cd2dc551-07ec-4dee-9159-ad76993b6c92
- date added to LUP
- 2021-11-07 19:58:51
- date last changed
- 2024-04-20 14:53:26
@article{cd2dc551-07ec-4dee-9159-ad76993b6c92,
abstract = {{<p>Cells synthesize proteins using 20 standard amino acids and expand their biochemical repertoire through intricate enzyme-mediated post-translational modifications (PTMs). PTMs can either be static and represent protein editing events or be dynamically regulated as a part of a cellular response to specific stimuli. Protein histidine methylation (Hme) was an elusive PTM for over 5 decades and has only recently attracted considerable attention through discoveries concerning its enzymology, extent, and function. Here, we review the status of the Hme field and discuss the implications of Hme in physiological and cellular processes. We also review the experimental toolbox for analysis of Hme and discuss the strengths and weaknesses of different experimental approaches. The findings discussed in this review demonstrate that Hme is widespread across cells and tissues and functionally regulates key cellular processes such as cytoskeletal dynamics and protein translation. Collectively, the findings discussed here showcase Hme as a regulator of key cellular functions and highlight the regulation of this modification as an emerging field of biological research.</p>}},
author = {{Jakobsson, Magnus E}},
issn = {{1083-351X}},
language = {{eng}},
number = {{4}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{The Journal of biological chemistry}},
title = {{Enzymology and significance of protein histidine methylation}},
url = {{http://dx.doi.org/10.1016/j.jbc.2021.101130}},
doi = {{10.1016/j.jbc.2021.101130}},
volume = {{297}},
year = {{2021}},
}