Post-translational protein acetylation: an elegant mechanism for bacteria to dynamically regulate metabolic functions
Post-translational modifications (PTM) decorate proteins to provide functional heterogeneity
to an existing proteome. The large number of known PTMs highlights the many ways that …
to an existing proteome. The large number of known PTMs highlights the many ways that …
[HTML][HTML] Sirtuin regulation in aging and injury
N Poulose, R Raju - Biochimica et Biophysica Acta (BBA)-Molecular Basis …, 2015 - Elsevier
Sirtuins or Sir2 family of proteins are a class of NAD+ dependent protein deacetylases which
are evolutionarily conserved from bacteria to humans. Some sirtuins also exhibit mono-ADP …
are evolutionarily conserved from bacteria to humans. Some sirtuins also exhibit mono-ADP …
Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation
The emerging view of Nε-lysine acetylation in eukaryotes is of a relatively abundant post-
translational modification (PTM) that has a major impact on the function, structure, stability …
translational modification (PTM) that has a major impact on the function, structure, stability …
Acylation of biomolecules in prokaryotes: a widespread strategy for the control of biological function and metabolic stress
KL Hentchel… - … and Molecular Biology …, 2015 - Am Soc Microbiol
Acylation of biomolecules (eg, proteins and small molecules) is a process that occurs in cells
of all domains of life and has emerged as a critical mechanism for the control of many …
of all domains of life and has emerged as a critical mechanism for the control of many …
Comprehensive Profiling of Protein Lysine Acetylation in Escherichia coli
K Zhang, S Zheng, JS Yang, Y Chen… - Journal of proteome …, 2013 - ACS Publications
Protein lysine acetylation plays a key role in regulating chromatin dynamics, gene
expression and metabolic pathways in eukaryotes, and, thus, contributes to diverse cellular …
expression and metabolic pathways in eukaryotes, and, thus, contributes to diverse cellular …
Protein acetylation in bacteria
CM VanDrisse… - Annual review of …, 2019 - annualreviews.org
Acetylation is a posttranslational modification conserved in all domains of life that is carried
out by N-acetyltransferases. While acetylation can occur on N α-amino groups, this review …
out by N-acetyltransferases. While acetylation can occur on N α-amino groups, this review …
Regulation, function, and detection of protein acetylation in bacteria
VJ Carabetta, IM Cristea - Journal of bacteriology, 2017 - Am Soc Microbiol
ABSTRACT N ε-Lysine acetylation is now recognized as an abundant posttranslational
modification (PTM) that influences many essential biological pathways. Advancements in …
modification (PTM) that influences many essential biological pathways. Advancements in …
Protein acetylation affects acetate metabolism, motility and acid stress response in Escherichia coli
S Castaño‐Cerezo, V Bernal, H Post… - Molecular systems …, 2014 - embopress.org
Although protein acetylation is widely observed, it has been associated with few specific
regulatory functions making it poorly understood. To interrogate its functionality, we …
regulatory functions making it poorly understood. To interrogate its functionality, we …
Acetylome analysis reveals diverse functions of lysine acetylation in Mycobacterium tuberculosis
F Liu, M Yang, X Wang, S Yang, J Gu, J Zhou… - Molecular & cellular …, 2014 - ASBMB
The lysine acetylation of proteins is a reversible post-translational modification that plays a
critical regulatory role in both eukaryotes and prokaryotes. Mycobacterium tuberculosis is a …
critical regulatory role in both eukaryotes and prokaryotes. Mycobacterium tuberculosis is a …
Bacterial protein acetylation: the dawning of a new age
Protein acetylation has historically been considered a predominantly eukaryotic
phenomenon. Recent evidence, however, supports the hypothesis that acetylation broadly …
phenomenon. Recent evidence, however, supports the hypothesis that acetylation broadly …