Article
Medical Laboratory Technology
Maria Del Carmen Navarro-Ruiz, Jaime Lopez-Alcala, Alberto Diaz-Ruiz, Sandra Diaz Del Moral, Carmen Tercero-Alcazar, Andrea Nieto-Calonge, Jose Lopez-Miranda, Francisco J. Tinahones, Maria M. Malagon, Rocio Guzman-Ruiz
Summary: Obesity is a rapidly growing pathological condition worldwide, with altered lipid accumulation in adipose tissue as one of the main causes. This study explores the molecular mechanisms of adipose tissue dysfunction in conditions of obesity and insulin resistance through the study of protein acetylation modifications. The results reveal different acetylation patterns in subcutaneous and omental adipose tissue, and the impact of acetylation on the function of FABP4, highlighting the molecular complexity of adipose tissue.
TRANSLATIONAL RESEARCH
(2022)
Article
Microbiology
Kristen M. Jew, Van Thi Bich Le, Kiana Amaral, Allysa Ta, Nina M. Nguyen May, Melissa Law, Nicole Adelstein, Misty L. Kuhn
Summary: Acetylation is a protein post-translational modification that can influence cellular processes. Two mechanisms of N epsilon-acetylation have been identified in bacteria - non-enzymatic/chemical acetylation and enzymatic acetylation. This study focused on determining the 3D location of lysine residues that are acetylated by E. coli enzymes and investigating their conservation in homologs. The results revealed discrepancies between linear amino acid sequences and 3D structures in assessing lysine residue conservation.
FRONTIERS IN MICROBIOLOGY
(2022)
Article
Chemistry, Multidisciplinary
Soeren Kirchgaessner, Michael B. Braun, Natascha Bartlick, Cengiz Koc, Christopher D. Reinkemeier, Edward A. Lemke, Thilo Stehle, Dirk Schwarzer
Summary: Lysine acetylation is a post-translational modification of proteins, and a 1,2,4-triazole amino acid (ApmTri) has been identified as a mimic for acetyllysine (Kac) to recruit bromodomains (Brds) of the BET family. The optimization of ApmTri substituents and side chain spacing enabled BET Brds to bind to ApmTri-containing peptides with affinities similar to native substrates. The use of genetically encoded ApmTri allowed the study of BET proteins in vitro and in vivo by providing a stable Kac mimic that reflects charge neutralization and Brd recruitment.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2023)
Article
Biology
Gonzalo Fernandez-Fuente, Katherine A. Overmyer, Alexis J. Lawton, Ildiko Kasza, Samantha L. Shapiro, Patricia Gallego-Munoz, Joshua J. Coon, John M. Denu, Caroline M. Alexander, Luigi Puglielli
Summary: In the cytosol, mitochondria and extracellular milieu can import citrate through SLC25A1 and SLC13A5. Citrate is used by ACLY to generate acetyl-CoA, which is then exported to the endoplasmic reticulum (ER) through SLC33A1. Mice with overexpression of SLC13A5 displayed a progeria-like phenotype and increased engagement of the ER acetylation machinery, while SLC25A1 overexpression did not show these phenotypes and engagement.
COMMUNICATIONS BIOLOGY
(2023)
Article
Agriculture, Multidisciplinary
Qibin Wu, Zhenxiang Li, Jingtao Yang, Fu Xu, Xueqin Fu, Liping Xu, Chuihuai You, Dongjiao Wang, Yachun Su, Youxiong Que
Summary: This study reports the first comprehensive analysis of protein lysine acetylation, 2-hydroxyisobutyrylation, and lysine lactylation in sugarcane. These post-translational modifications were found to be involved in energy metabolism and stress response. The results provide new insights into the molecular mechanisms of protein PTMs in sugarcane.
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
(2023)
Review
Microbiology
Michael Lammers
Summary: Ac(et)ylation is a significant post-translational modification affecting essential cellular processes in all domains of life. It can occur at the ε-amino group of lysine side chains or at the α-amino group of proteins, and is involved in regulating protein function through various mechanisms including charge quenching, size alteration of lysine side chains, and interference with other modifications.
FRONTIERS IN MICROBIOLOGY
(2021)
Article
Biochemical Research Methods
Qianqian Han, Feng Chen, Shushan Liu, Yushu Ge, Jiang Wu, Dan Liu
Summary: This study developed a gene-coding protein sensor based on the mechanism of fluorescence resonance energy transfer for detecting H4 lysine acetylation levels. Different sensors with varying substrate sequences were found to increase response efficiency, while single-site lysine mutation did not significantly decrease efficiency. Inhibitors and histone deacetylase added to the system showed effects on the sensor's response.
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
(2021)
Article
Clinical Neurology
Ya-Wen Xu, Peng Lin, Shu-Fa Zheng, Wen Huang, Zhang-Ya Lin, Huang-Cheng Shang-Guan, Yuan-Xiang Lin, Pei-Sen Yao, De-Zhi Kang
Summary: The study identified dynamic changes in protein lysine acetylation levels during glioma-associated seizures and confirmed the important role of acetylation in metabolic processes. Additionally, key enzymes and proteins associated with acetylation during seizures were identified.
FRONTIERS IN NEUROLOGY
(2021)
Article
Immunology
Jun-meng Wang, Si-rui Lin, Yuan-bing Zhu, Jing Yuan, Yue-mei Wang, Qun Zhang, Lu-shuang Xie, Si-hui Li, Shu-qing Liu, Shu-guang Yu, Qiao-feng Wu
Summary: This study identified 2597 acetylation events and 1914 sites in the UC model, revealing enrichment of differentially acetylated proteins in pathways like TCA cycle, fatty acid metabolism, and protein processing in the endoplasmic reticulum. Furthermore, it showed the potential role of HSP90B1-K142ac in the pathogenesis of UC.
INTERNATIONAL IMMUNOPHARMACOLOGY
(2021)
Article
Microbiology
Junlin Wang, Huanying Pang, Linlin Yin, Fuyuan Zeng, Na Wang, Rowena Hoare, Sean J. Monaghan, Wanxin Li, Jichang Jian
Summary: Protein lysine acetylation is an evolutionarily conserved post-translational modification that plays a crucial role in the metabolism and virulence of V. mimicus. This study provides a comprehensive analysis of the protein lysine acetylome in V. mimicus and establishes an important foundation for further research on the biological function of lysine acetylation in V. mimicus.
FRONTIERS IN MICROBIOLOGY
(2022)
Article
Biochemistry & Molecular Biology
Giordano Proietti, Yali Wang, Chiara Punzo, Jasmin Mecinovic
Summary: KAT8 is capable of acetylating selective lysine analogues with subtle changes in side chains and main chains, in addition to natural lysine. This study contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase family.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Microbiology
Osama A. Abdalla, Akhtar Ali
Summary: This study collected 57 isolates of Watermelon mosaic virus (WMV) from cucurbit fields in nine southern states, and found high sequence identities among them. Phylogenetic analysis revealed that all U.S. WMV isolates belong to Group 3, with two clusters similar to previously reported subgroups and a new distinct subgroup formed in this study. Analysis showed low non-synonymous to synonymous nucleotide substitution ratio, indicating negative purifying selection in the CP gene of WMV.
Article
Environmental Sciences
Lei Lei, Jumei Zeng, Lingyun Wang, Tao Gong, Xin Zheng, Wei Qiu, Ru Zhang, Libing Yun, Yingming Yang, Yuqing Li
Summary: The study identified the acetylome of S. mutans and compared the quantitative acetylome analysis between bacterial biofilm growth and planktonic growth. The dynamic changes of protein acetylation were quantified using TMT labeling and Kac affinity enrichment. The results showed that the acetylation of lysine in proteins varies during biofilm development, revealing a potential regulatory mechanism for glucosyltransferases function.
ENVIRONMENTAL MICROBIOLOGY REPORTS
(2021)
Article
Biochemical Research Methods
Eunji Sung, Hyunchae Sim, Young-Chang Cho, Wonhwa Lee, Jong-Sup Bae, Minjia Tan, Sangkyu Lee
Summary: In this study, the authors identified acetylation and lactylation sites in Kupffer cells using global acylome technology. They found differences in the subcellular distributions and sequence motifs of modified proteins. Functional enrichment analyses provided insights into the roles of these modifications.
JOURNAL OF PROTEOME RESEARCH
(2023)
Article
Microbiology
Yanwei Gong, Ying Li, Dongyang Liu, Lianqiang Jiang, Hui Liang, Yuanhua Wu, Fenglong Wang, Jinguang Yang
Summary: Kac is a model for all acylation modification studies and is involved in six major biological functions. In this study, we investigated the acetylation modification of proteins in healthy and TSWV-infected N. benthamiana leaves. Our results showed that acetylation of proteins was significantly altered after the infection, with upregulated and downregulated sites. We also identified conserved motifs and found that most of the Kac proteins were located in the chloroplast and cytoplasm, participating in cellular and metabolic processes.
FRONTIERS IN MICROBIOLOGY
(2023)
