Results 51 to 60 of about 182,599 (256)

The Nuclear Localization of ACLY Guards Early Embryo Development Through Recruiting P300 and HAT1 to Promote Histone Acetylation and Transcription

Advanced Science, EarlyView.
ACLY is vital for early embryo development. IGF‐1 activates AKT to phosphorylate ACLY, driving its nuclear localization and recruitment of HATs (P300/HAT1), boosting acetyl‐CoA production and histone acetylation for transcriptional activation. Conversely, ACLY deficiency (via knockdown, knockout, or AKT inhibition) reduces nuclear acetyl‐CoA, disrupts ...
Yerong Ma, Yingyi Zhang, Weijie Yang, Xiaomei Tong, Siya Liu, Yan Zhou, Mengjia Qiu, Huifang Jiang, Zhanhong Hu, Peipei Ren, Yan Rong, Mengru Lai, Jiamin Jin, Fei Huang, Liujian Ouyang, Feng Zhou, Heng‐Yu Fan, Yin‐Li Zhang, Songying Zhang   +18 more
wiley   +1 more source

Structure of the Histone Acetyltransferase Hat1 [PDF]

Cell, 1998
We have solved the crystal structure of the yeast histone acetyltransferase Hat1-acetyl coenzyme A (AcCoA) complex at 2.3 A resolution. Hat1 has an elongated, curved structure, and the AcCoA molecule is bound in a cleft on the concave surface of the protein, marking the active site of the enzyme.
Rolf Sternglanz, Venki Ramakrishnan, Robert N Dutnall, Stefan T. Tafrov   +3 more
openaire   +3 more sources

Class I histone deacetylases (HDAC1–3) are histone lysine delactylases

bioRxiv, 2021
Lysine l-lactylation [K(l-la)] is a newly discovered histone mark that can be stimulated under conditions of high glycolysis, such as the Warburg effect. K(l-la) is associated with functions that are different from the widely studied histone acetylation.
Carlos Moreno-Yruela, Di Zhang, Wei Wei, Michael Bæk, Wenchao Liu, Jinjun Gao, D. Danková, Alexander L. Nielsen, Julie E Bolding, Lu Yang, Samuel T. Jameson, J. Wong, C. Olsen, Yingming Zhao   +13 more
semanticscholar   +1 more source

MYC Binding Near Transcriptional End Sites Regulates Basal Gene Expression, Read‐Through Transcription, and Intragenic Contacts

Advanced Science, EarlyView.
MYC is a transcription factor (TF) that binds DNA near transcriptional start sites (TSSs) and within enhancer elements. Here, unappreciated sites of MYC binding in the vicinity of transcriptional end sites (TESs) of many genes in multiple cell types in association with numerous other TFs are described previously.
Huabo Wang, Bingwei Ma, Taylor Stevens, Jessica Knapp, Jie Lu, Edward V. Prochownik   +5 more
wiley   +1 more source

G9a-mediated methylation of ERα links the PHF20/MOF histone acetyltransferase complex to hormonal gene expression

Nature Communications, 2016
The euchromatin histone methyltransferase 2 (also known as G9a) methylates histone H3K9 to repress gene expression, but it also acts as a coactivator for some nuclear receptors. The molecular mechanisms underlying this activation remain elusive.
Xi Zhang, Danni Peng, Y. Xi, C. Yuan, Cari A. Sagum, B. J. Klein, Kaori Tanaka, H. Wen, T. Kutateladze, Wei Li, M. Bedford, Xiaobing Shi   +11 more
semanticscholar   +1 more source

Post‐Translational Modifications in Cilia and Ciliopathies

Advanced Science, EarlyView.
This review synthesizes current understanding of post‐translational modifications (PTMs) in ciliary proteins and emphasizes their roles in ciliary formation, homeostasis, and signaling. This review also discusses the implication of PTM dysregulation in ciliopathies and explores therapeutic strategies targeting PTM‐modifying enzymes.
Jie Ran, Jun Zhou
wiley   +1 more source

The Functional Analysis of Histone Acetyltransferase MOF in Tumorigenesis

International Journal of Molecular Sciences, 2016
Changes in chromatin structure and heritably regulating the gene expression by epigenetic mechanisms, such as histone post-translational modification, are involved in most cellular biological processes.
Jiaming Su, Fei Wang, Yong Cai, Jingji Jin   +3 more
semanticscholar   +1 more source

Histone Demethylase UTX Suppresses Tumor Cell Proliferation by Regulating Stress Granules

Advanced Science, EarlyView.
These findings indicate that cytoplasmic UTX forms puncta and co‐localizes in stress granules (SGs) upon various stresses. UTX TPR‐domain‐dependently and demethylase‐activity‐independently destabilize SGs by binding G3BP1, the SG hub protein, to disrupt SG network, thus affects tumorigenesis.
Xikai Liu, Xinran Liu, Mei Xue, Yushuo Xiao, Yuchen Chen, Rong Qiu, Di Wu, Yihao Zhou, Jiao Wang, Yan Yuan, Linwei Yu, Tianyi Shi, Yangkai Li, Hua Su, Hong Chen, Yong Liu, Kun Huang, Ling Zheng   +17 more
wiley   +1 more source

Enzyme kinetics and inhibition of histone acetyltransferase KAT8 [PDF]

European Journal of Medicinal Chemistry, 2015
Lysine acetyltransferase 8 (KAT8) is a histone acetyltransferase (HAT) responsible for acetylating lysine 16 on histone H4 (H4K16) and plays a role in cell cycle progression as well as acetylation of the tumor suppressor protein p53. Further studies on its biological function and drug discovery initiatives will benefit from the development of small ...
Wapenaar, Hannah, van der Wouden, Petra E, Groves, Matthew R, ROTILI, Dante, MAI, Antonello, Dekker, Frank J.   +5 more
openaire   +3 more sources

Molecular Basis for Histone Acetyltransferase Regulation by Binding Partners, Associated Domains, and Autoacetylation.

ACS Chemical Biology, 2016
Acetylation is a post-translational modification (PTM) that regulates chromatin dynamics and function. Dysregulation of acetylation or acetyltransferase activity has been correlated with several human diseases.
C. McCullough, R. Marmorstein
semanticscholar   +1 more source