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Karen Chen, Seth A Bennett, Navin Rana, Huda Yousuf, Mohamed Said, Sadiqa Taaseen, Natalie Mendo, Steven Marc Meltser, Mariana Torrente
Amyotrophic Lateral Sclerosis (ALS) and Parkinson's disease (PD) are devastating neurodegenerative diseases involving the progressive degeneration of neurons. No cure is available for patients diagnosed with these diseases. A prominent feature for both ALS and PD is the accumulation of protein inclusions in the cytoplasm of degenerating neurons; however, the particular protein comprising these inclusions varies. The RNA-binding proteins TDP-43 and FUS are most notable in ALS, while α-synuclein aggregates into Lewy bodies in PD...
December 15, 2017: ACS Chemical Neuroscience
Florian Cymer, Hermann Beck, Adelheid Rohde, Dietmar Reusch
Therapeutic antibodies (IgG-type) contain several post-translational modifications (PTMs) whereby introducing a large heterogeneity, both structural and functional, into this class of therapeutics. Of these modifications, glycosylation in the fragment crystallizable (Fc) region is the most heterogeneous PTM, which can affect the stability of the molecule and interactions with Fc-receptors in vivo. Hence, the glycoform distribution can affect the mode of action and have implications for bioactivity, safety and efficacy of the drug...
November 24, 2017: Biologicals: Journal of the International Association of Biological Standardization
Juan Casado, Paula Mayorga Burrezo, Carlos Franco, Ruben Caballero, Marta Mas, Fernando Langa, Juan T Lopez Navarrete, Concepció Rovira, Jaume Veciana
: A detailed analysis of positive charged species generated on a series of thienylenevinylene (nTV) wires terminally substituted with two perchlorotriphenylmethyl (*PTM) radical acceptors groups, *PTM-nTV-PTM* (n = 2-7), has been carried out. Motivated by the counterintuitively key role played by holes in the nTV bridges on the operating mechanism of electron transfer in their radi-cal-anion mixed-valence derivatives, a wide combination of experimental and theoretical techniques have been used, aiming to get further insights on their structural location...
December 14, 2017: Chemistry: a European Journal
Manabu Koike, Yasutomo Yutoku, Aki Koike
Molecularly targeted therapies have high specificity and significant cancer-killing effect. However, their antitumor effect might be greatly diminished by variation in even a single amino acid in the target site, as it occurs, for example, as a consequence of SNPs. Increasing evidence suggests that the DNA repair protein Ku80 is an attractive target molecule for the development of next-generation radiosensitizers for human cancers. However, the localization, post-translational modifications (PTMs), and complex formation of Ku80 have not been elucidated in canines...
December 2017: FEBS Open Bio
Atsushi Yokoyama, Shogo Katsura, Akira Sugawara
Posttranslational modification (PTM) of proteins is used to regulate protein activity and stability. Histone PTMs are regarded as some of the most important, as they can directly regulate gene expression through chromatin reorganization. Recently, histone proteins were found to undergo succinylation, adding to other well-known PTMs such as acetylation, methylation, and phosphorylation. However, there is little information regarding the enzyme which catalyzes histone lysine succinylation. In fact, it is unclear whether this reaction is enzymatic...
2017: Biochemistry Research International
Michelle Quezada, Cuauhtemoc Licona-Cassani, Pablo Cruz-Morales, Angela A Salim, Esteban Marcellin, Robert J Capon, Francisco Barona-Gómez
Streptomyces are Gram-positive bacteria that occupy diverse ecological niches including host-associations with animals and plants. Members of this genus are known for their overwhelming repertoire of natural products, which has been exploited for almost a century as a source of medicines and agrochemicals. Notwithstanding intense scientific and commercial interest in Streptomyces natural products, surprisingly little is known of the intra- and/or inter-species ecological roles played by these metabolites. In this report we describe the chemical structures, biological properties, and biosynthetic relationships between natural products produced by Streptomyces isolated from internal tissues of predatory Conus snails, collected from the Great Barrier Reef, Australia...
2017: Frontiers in Microbiology
Hongik Hwang, Hyewhon Rhim
Post-translational modifications (PTMs) covalently modify proteins and diversify protein functions. Along with protein phosphorylation, another common PTM is the addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine and/or threonine residues. O-GlcNAc modification is similar to phosphorylation in that it occurs to serine and threonine residues and cycles on and off with a similar time scale. However, a striking difference is that the addition and removal of the O-GlcNAc moiety on all substrates are mediated by the two enzymes regardless of proteins, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), respectively...
December 6, 2017: Pharmacological Research: the Official Journal of the Italian Pharmacological Society
Kyle K Biggar, Zhentian Wang, Shawn S-C Li
Lysine methylation is a prevalent post-translational modification (PTM) used by the cell to reversibly regulate protein function. Although it has been extensively studied in the context of histones and the associated chromatin, the remaining methyllysine proteome remains largely unexplored. This SnapShot provides an overview of the current state of lysine methylation research and its emergence as a dynamic PTM occurring on histone and non-histone proteins.
December 7, 2017: Molecular Cell
Carsten Janke, Guillaume Montagnac
Among the different types of cytoskeletal components, microtubules arguably accumulate the greatest diversity of post-translational modifications (PTMs). Acetylation of lysine 40 (K40) of α-tubulin has received particular attention because it is the only tubulin PTM to be found in the lumen of microtubules: most other tubulin PTMs are found at the outer surface of the microtubule. As a consequence, the enzyme catalyzing K40 acetylation needs to penetrate the narrow microtubule lumen to find its substrate. Acetylated microtubules have been considered to be stable, long-lived microtubules; however, until recently, there was little information about whether the longevity of these microtubules is the cause or the consequence of acetylation...
December 4, 2017: Current Biology: CB
Fa Zhang, Shutao Ma
BACKGROUND: Histone acetylation is an essential way of post-translational modification (PTM) and a significant component of epigenetic regulation that is mediated by Bromodomain-containing protein (BRD). In recent years, many researchers have found that a variety of malignancy, inflammatory and other diseases occurrence and development are associated with BRD4 expression disorders or dysfunction. Meanwhile, many the bromodomain inhibitors of the bromodomains and extra-terminal (BET) family is reported in many papers...
November 29, 2017: Current Drug Targets
Mattis Kupferschmid, Moyira Osny Aquino-Gil, Hosam Shams-Eldin, Jörg Schmidt, Nao Yamakawa, Frédéric Krzewinski, Ralph T Schwarz, Tony Lefebvre
BACKGROUND: Post-translational modifications (PTMs) constitute a huge group of chemical modifications increasing the complexity of the proteomes of living beings. PTMs have been discussed as potential anti-malarial drug targets due to their involvement in many cell processes. O-GlcNAcylation is a widespread PTM found in different organisms including Plasmodium falciparum. The aim of this study was to identify O-GlcNAcylated proteins of P. falciparum, to learn more about the modification process and to understand its eventual functions in the Apicomplexans...
November 29, 2017: Malaria Journal
Giorgia Spaggiari, Giulia Brigante, Sara De Vincentis, Umberto Cattini, Laura Roli, Maria Cristina De Santis, Enrica Baraldi, Simonetta Tagliavini, Manuela Varani, Tommaso Trenti, Vincenzo Rochira, Manuela Simoni, Daniele Santi
Purpose: The relationship between probiotics and levothyroxine (LT4) requirement has not yet been investigated. The aim of this study was to assess whether a mixture of highly charged Lactobacilli and Bifidobacteria (VSL#3®) is able to influence LT4 metabolism acting on the gut microbiota. Methods: A prospective, randomized, single-blind, controlled, investigator-started clinical trial was carried out. Patients with primary hypothyroidism were randomly assigned to the study (VSL#3® + LT4) and the control group (LT4)...
2017: Frontiers in Endocrinology
Daniel L Winter, Gene Hart-Smith, Marc R Wilkins
Protein methylation is one of the major post-translational modifications (PTMs) in the cell. In Saccharomyces cerevisiae, over twenty protein methyltransferases (MTases) and their respective substrates have been identified. However, the way in which these MTases are modified, and potentially subject to regulation, remains poorly understood. Here, we investigated six overexpressed S. cerevisiae protein MTases (Rkm1, Rkm4, Efm4, Efm7, Set5 and Hmt1) to identify PTMs of potential functional relevance. We identified 48 PTM sites across the six MTases, including phosphorylation, acetylation and methylation...
November 25, 2017: Journal of Molecular Biology
Isabelle Devambez, Juliette van Dijk, Salim Benlefki, Sophie Layalle, Yves Grau, Krzysztof Rogowski, Marie-Laure Parmentier, Laurent Soustelle
Microtubules (MTs) play crucial roles during neuronal life. They are formed by heterodimers of alpha and beta-tubulins, which are subjected to several post-translational modifications (PTMs). Amongst them, glutamylation consists in the reversible addition of a variable number of glutamate residues to the C-terminal tails of tubulins. Glutamylation is the most abundant MT PTM in the mammalian adult brain, suggesting that it plays an important role in the nervous system (NS). Here, we show that the previously uncharacterized CG31108 gene encodes an alpha-tubulin glutamylase acting in the Drosophila NS...
November 24, 2017: Scientific Reports
Aurore M-F Delachat, Nora Guidotti, Andreas L Bachmann, Antonio C A Meireles-Filho, Horst Pick, Carolin C Lechner, Cédric Deluz, Bart Deplancke, David M Suter, Beat Fierz
The regulation of fundamental processes such as gene expression or cell differentiation involves chromatin states, demarcated by combinatorial histone post-translational modification (PTM) patterns. The subnuclear organization and dynamics of chromatin states is not well understood, as tools for their detection and modulation in live cells are lacking. Here, we report the development of genetically encoded chromatin-sensing multivalent probes, cMAPs, selective for bivalent chromatin, a PTM pattern associated with pluripotency in embryonic stem cells (ESCs)...
November 21, 2017: Cell Chemical Biology
Bernhard Lüscher, Mareike Bütepage, Laura Eckei, Sarah Krieg, Patricia Verheugd, Brian H Shilton
Posttranslational modifications (PTMs) regulate protein functions and interactions. ADP-ribosylation is a PTM, in which ADP-ribosyltransferases use nicotinamide adenine dinucleotide (NAD+) to modify target proteins with ADP-ribose. This modification can occur as mono- or poly-ADP-ribosylation. The latter involves the synthesis of long ADP-ribose chains that have specific properties due to the nature of the polymer. ADP-Ribosylation is reversed by hydrolases that cleave the glycosidic bonds either between ADP-ribose units or between the protein proximal ADP-ribose and a given amino acid side chain...
November 27, 2017: Chemical Reviews
Matthias C Truttmann, Hidde L Ploegh
Post-translational protein modifications (PTMs) orchestrate the activity of individual proteins and ensure their proper function. While modifications such as phosphorylation or glycosylation are well understood, more unusual modifications, including nitrosylation or AMPylation remain comparatively poorly characterized. Research on protein AMPylation-which refers to the covalent addition of an AMP moiety to the side chains of serine, threonine or tyrosine-has undergone a renaissance (Yarbrough et al., 2009; Engel et al...
July 20, 2017: Bio-protocol
Sam L Ivry, Nicole O Meyer, Michael B Winter, Markus F Bohn, Giselle M Knudsen, Anthony J O'Donoghue, Charles S Craik
Enzymes that modify the proteome, referred to as post-translational modifying (PTM) enzymes, are central regulators of cellular signaling. Determining the substrate specificity of PTM enzymes is a critical step in unraveling their biological functions both in normal physiological processes and in disease states. Advances in peptide chemistry over the last century have enabled the rapid generation of peptide libraries for querying substrate recognition by PTM enzymes. In this review, we highlight various peptide-based approaches for analysis of PTM enzyme substrate specificity...
November 23, 2017: Protein Science: a Publication of the Protein Society
Ebru Ercan, Sameh Eid, Christian Weber, Alexandra Kowalski, Maria Bichmann, Annika Behrendt, Frank Matthes, Sybille Krauss, Peter Reinhardt, Simone Fulle, Dagmar E Ehrnhoefer
BACKGROUND: Tau is a microtubule-binding protein, which is subject to various post-translational modifications (PTMs) including phosphorylation, methylation, acetylation, glycosylation, nitration, sumoylation and truncation. Aberrant PTMs such as hyperphosphorylation result in tau aggregation and the formation of neurofibrillary tangles, which are a hallmark of Alzheimer's disease (AD). In order to study the importance of PTMs on tau function, antibodies raised against specific modification sites are widely used...
November 21, 2017: Molecular Neurodegeneration
Wankun Deng, Lili Ma, Ying Zhang, Jiaqi Zhou, Yongbo Wang, Zexian Liu, Yu Xue
Macroautophagy/autophagy is a highly conserved process for degrading cytoplasmic contents, determines cell survival or death, and regulates the cellular homeostasis. Besides ATG proteins, numerous regulators together with various post-translational modifications (PTMs) are also involved in autophagy. In this work, we collected 4,237 experimentally identified proteins regulated in autophagy and cell death pathways from the literature. Then we computationally identified potential orthologs of known proteins, and developed a comprehensive database of The Autophagy, Necrosis, ApopTosis OrchestratorS (THANATOS, http://thanatos...
November 20, 2017: Autophagy
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