2018
https://www.ncbi.nlm.nih.gov/pubmed/29887264
Xu JY, Xu Y, Xu Z, Zhai LH, Ye Y, Zhao Y, Chu X, Tan M, Ye BC.
Cell Chem Biol. 2018 May 21. pii: S2451-9456(18)30152-1. doi: 10.1016/j.chembiol.2018.05.005. [Epub ahead of print] PMID: 29887264
2.
Revealing the protein propionylation activity of the histone acetyltransferase MOF (males absent on the first). Han
Z, Wu H, Kim S, Yang X, Li Q, Huang H, Cai H, Bartlett MG, Dong A, Zeng
H, Brown PJ, Yang XJ, Arrowsmith CH, Zhao Y, Zheng YG.
J Biol Chem. 2018 Mar 2;293(9):3410-3420. doi: 10.1074/jbc.RA117.000529. Epub 2018 Jan 10. PMID: 29321206
3.
Liu X, Wei W, Liu Y, Yang X, Wu J, Zhang Y, Zhang Q, Shi T, Du JX, Zhao Y, Lei M, Zhou JQ, Li J, Wong J. Cell Discov. 2017 May 23;3:17016. doi: 10.1038/celldisc.2017.16. eCollection 2017. PMID:28580166
".. Recent studies indicate that histones are subjected to various types of
acylation including acetylation, propionylation and crotonylation."
4.
Nie L, Shuai L, Zhu M, Liu P, Xie ZF, Jiang S, Jiang HW, Li J, Zhao Y, Li JY, Tan M.
Mol Cell Proteomics. 2017 Jul;16(7):1324-1334. doi: 10.1074/mcp.M117.067553. Epub 2017 Apr 27.PMID:28450421
".. Type 2 diabetes (T2D) is a major chronic healthcare concern worldwide.
Emerging evidence suggests that a histone-modification-mediated
epigenetic mechanism underlies T2D."
5.
Li QQ, Hao JJ, Zhang Z, Krane LS, Hammerich KH, Sanford T, Trepel JB, Neckers L, Agarwal PK.
Sci Rep. 2017 Mar 15;7(1):201. doi: 10.1038/s41598-017-00143-6. PMID: 28298630
".. Furthermore, quantitative proteome studies identified 14 types of PTMs
with 93 marks on the core histones, including 34 novel histone marks of
butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation,
O-GlcNAcylation, propionylation, and succinylation in AUY922- and
ganetespib-treated 5637 cells".
6.
Pelletier N, Grégoire S, Yang XJ.
Curr Protoc Protein Sci. 2017 Feb 2;87:14.11.1-14.11.18. doi: 10.1002/cpps.26. PMID:28150880
".. Lysine acetylation refers to addition of an acetyl moiety to the
epsilon-amino group of a lysine residue and is important for regulating
protein functions in various organisms from bacteria to humans. This is a
reversible and precisely controlled covalent modification that either
serves as an on/off switch or participates in a codified manner with
other post-translational modifications to regulate different cellular
and developmental processes in normal and pathological states. This unit
describes methods for in vitro and in vivo determination of lysine
acetylation. Such methods can be easily extended for analysis of other
acylations (such as propionylation, butyrylation, crotonylation, and
succinylation) that are also present in histones and many other
proteins."
2016
7.
Sabari BR, Zhang D, Allis CD, Zhao Y.
Nat Rev Mol Cell Biol. 2017 Feb;18(2):90-101. doi: 10.1038/nrm.2016.140. Epub 2016 Dec 7. Review. PMID: 27924077
" Eight types of short-chain Lys acylations have recently been identified
on histones: propionylation, butyrylation, 2-hydroxyisobutyrylation,
succinylation, malonylation, glutarylation, crotonylation and
β-hydroxybutyrylation. Emerging evidence suggests that these histone
modifications affect gene expression and are structurally and
functionally different from the widely studied histone Lys acetylation.
In this Review, we discuss the regulation of non-acetyl histone
acylation by enzymatic and metabolic mechanisms, the acylation 'reader'
proteins that mediate the effects of different acylations and their
physiological functions, which include signal-dependent gene activation,
spermatogenesis, tissue injury and metabolic stress. We propose a model
to explain our present understanding of how differential histone
acylation is regulated by the metabolism of the different acyl-CoA
forms, which in turn modulates the regulation of gene expression".
8.
Sun M, Xu J, Wu Z, Zhai L, Liu C, Cheng Z, Xu G, Tao S, Ye BC, Zhao Y, Tan M.
J Proteome Res. 2016 Dec 2;15(12):4696-4708. Epub 2016 Nov 10.PMID:27804304
", we identified 1467 lysine propionylation sites in 603 proteins in E.
coli. Quantitative propionylome analysis further revealed that global
lysine propionylation level was drastically increased in response to
propionate treatment,.."
9.
Xiong X, Panchenko T, Yang S, Zhao S, Yan P, Zhang W, Xie W, Li Y, Zhao Y, Allis CD, Li H.
Nat Chem Biol. 2016 Dec;12(12):1111-1118. doi: 10.1038/nchembio.2218. Epub 2016 Oct 24. PMID: 27775714
".. Recognition of histone covalent modifications by 'reader' modules
constitutes a major mechanism for epigenetic regulation. A recent
upsurge of newly discovered histone lysine acylations, such as
crotonylation (Kcr), butyrylation (Kbu), and propionylation (Kpr),
greatly expands the coding potential of histone lysine modifications.
Here we demonstrate that the histone acetylation-binding double PHD
finger (DPF) domains of human MOZ (also known as KAT6A) and DPF2 (also
known as BAF45d) accommodate a wide range of histone lysine acylations
with the strongest preference for Kcr.
10.
Li Y, Sabari BR, Panchenko T, Wen H, Zhao D, Guan H, Wan L, Huang H, Tang Z, Zhao Y, Roeder RG, Shi X, Allis CD, Li H.Mol Cell. 2016 Apr 21;62(2):181-193. doi: 10.1016/j.molcel.2016.03.028.PMID: 27105114Free PMC Article
" Recognition of histone covalent modifications by chromatin-binding
protein modules ("readers") constitutes a major mechanism for epigenetic
regulation, typified by bromodomains that bind acetyllysine. Non-acetyl
histone lysine acylations (e.g., crotonylation, butyrylation,
propionylation) have been recently identified, but readers that prefer
these acylations have not been characterized. Here we report that the
AF9 YEATS domain displays selectively higher binding affinity for
crotonyllysine over acetyllysine."
2014
11.
Wu Z, Cheng Z, Sun M, Wan X, Liu P, He T, Tan M, Zhao Y.
Mol Cell Proteomics. 2015 Feb;14(2):329-39. doi: 10.1074/mcp.M114.044255. Epub 2014 Dec 11.PMID:25505155
12.
Tooley JG, Schaner Tooley CE.
Protein Sci. 2014 Dec;23(12):1641-9. doi: 10.1002/pro.2547. Epub 2014 Sep 26. Review.PMID:25209108
".. Historically considered static regulators of protein stability,
additional functional roles for N-terminal PTMs are now beginning to be
elucidated. New findings show that N-terminal methylation, along with
N-terminal acetylation, is an important regulatory modification with
significant roles in development and disease progression.There are also emerging studies on the enzymology and functional roles
of N-terminal ubiquitylation and N-terminal propionylation.
13.
Lee S.Toxicol Res. 2013 Jun;29(2):81-6. doi: 10.5487/TR.2013.29.2.081. Review. PMID:24278632
".. Post-translational modification (PTM) alters the three-dimensional (3D)
structure of proteins by covalently binding small molecules to them and
therefore represents a major protein function diversification mechanism.
Because of the crucial roles PTM plays in biological systems, the
identification of novel PTMs and study of the role of PTMs are gaining
much attention in proteomics research. Of the 300 known PTMs, protein
acylation, including lysine formylation, acetylation, propionylation,
butyrylation, malonylation, succinylation, and crotonylation, regulates
the crucial functions of many eukaryotic proteins involved in cellular
metabolism, cell cycle, aging, growth, angiogenesis, and cancer."
14.
Singh B, Boopathy S, Somasundaram K, Umapathy S.
J Biophotonics. 2012 Mar;5(3):230-9. doi: 10.1002/jbio.201100061. Epub 2012 Jan 19. PMID:22259119
"Histone deacetylase inhibitors (HDIs) have attracted considerable
attention as potential drug molecules in tumour biology. In order to
optimise chemotherapy, it is important to understand the mechanisms of
regulation of histone deacetylase (HDAC) enzymes and modifications
brought by various HDIs."
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