Front Cover
Cover illustration By optimising the efficiency of experimental procedures, we can minimise the lab ’s environmental footprint, making research more sustainable. Read more in Penndorf and Jabs ‘A new approach to making scientific research more efficient ’ rethinking sustainability’ in this issue. (Source: FEBS Letters)
Source: FEBS Letters - October 9, 2023 Category: Biochemistry Tags: Issue Information Source Type: research
SUMO in the regulation of DNA repair and transcription at nuclear pores
This review focuses on the importance of sumoylation and SUMO-dependent ubiquitination in the relocalization/targeting of different types of DNA damage, stalled replication forks, telomeres and both activated and repressed genes to the nuclear periphery. The enrichment of proteasome at the nuclear envelope and association of SUMO proteases with nuclear pore complexes facilitate DNA repair pathway choice and optimal transcription regulation. AbstractTwo related post-translational modifications, the covalent linkage of Ubiquitin and the Small Ubiquitin-related MOdifier (SUMO) to lysine residues, play key roles in the regulat...
Source: FEBS Letters - October 8, 2023 Category: Biochemistry Authors: Susan M. Gasser,
Fran çoise Stutz Tags: Review Source Type: research
Evolutionarily conserved cysteines in plant cytosolic seryl ‐tRNA synthetase are important for its resistance to oxidation
We have examined the role of the disulfide link between evolutionarily conserved cysteines in plant cytosolic seryl-tRNA synthetase. We have identified features of the protein microenvironment which may promote disulfide bond formation in oxidizing conditions. Activity assays showed that the disulfide link is important for protein resistance to oxidation, which may be beneficial for translation during oxidative stress conditions in plants. We have previously identified a unique disulfide bond in the crystal structure ofArabidopsis cytosolic seryl-tRNA synthetase involving cysteines evolutionarily conserved in all green pla...
Source: FEBS Letters - October 7, 2023 Category: Biochemistry Authors: Valentina Evic,
Ruzica Soic,
Marko Mocibob,
Mario Kekez,
Josef Houser,
Michaela Wimmerov á,
Dubravka Matković‐Čalogović,
Ita Gruic‐Sovulj,
Ivana Kekez,
Jasmina Rokov‐Plavec Tags: Research Article Source Type: research
Design and engineering of artificial biosynthetic pathways —where do we stand and where do we go?
Microbial production of commodity and specialty chemicals has the potential to decrease our reliance on fossil fuels and reduce the accompanying environmental effects. The scope of traditional biomanufacturing can be greatly enhanced by constructing new-to-nature pathways toward target chemicals. Here, we outline the principles of artificial pathway design and engineering, highlight notable examples and provide an outlook on its future. The production of commodity and specialty chemicals relies heavily on fossil fuels. The negative impact of this dependency on our environment and climate has spurred a rising demand for mor...
Source: FEBS Letters - October 7, 2023 Category: Biochemistry Authors: Nika Sokolova,
Bo Peng,
Kristina Haslinger Tags: Review Source Type: research
Siderophore specificities of the Pseudomonas aeruginosa TonB ‐dependent transporters ChtA and ActA
Iron is a key nutrient for the growth of almost all bacteria. The pathogenPseudomonas aeruginosa is able to express at least 15 different iron acquisition pathways, each involving a specific outer membrane transporter. Most of these iron-uptake pathways rely on small iron chelators (siderophores) produced by other microorganisms. We identified the outer membrane transporters involved in the uptake of ironvia two α-carboxylate siderophores and three mixed α-carboxylate/hydroxamate siderophores. Iron is an essential nutrient for the survival and virulence ofPseudomonas aeruginosa. The pathogen expresses at least 15 diff...
Source: FEBS Letters - October 7, 2023 Category: Biochemistry Authors: Virginie Will,
V éronique Gasser,
Lauriane Kuhn,
Sarah Fritsch,
David E. Heinrichs,
Isabelle J. Schalk Tags: Research Letter Source Type: research
Structural view on autophagosome formation
Autophagy is a conserved intracellular degradation system in eukaryotes, involving the sequestration of degradation targets into autophagosomes. Autophagosome formation and cargo selectivity rely on core Atg proteins and cargo receptors, respectively. In this review, I cover the 30-year history of structural studies on core Atg proteins and cargo receptors and discuss the molecular mechanisms of autophagosome formation and selective autophagy. Autophagy is a conserved intracellular degradation system in eukaryotes, involving the sequestration of degradation targets into autophagosomes, which are subsequently delivered to l...
Source: FEBS Letters - October 6, 2023 Category: Biochemistry Authors: Nobuo N. Noda Tags: Review Source Type: research
RANBP2 Evolution and Human Disease
RAN binding protein 2 (RANBP2/Nup358) is a cytoplasmic filament nucleoporin involved in various cellular processes, such as nucleocytoplasmic transport and post-translational modifications. This review comprehensively discusses how dysregulation or mutation of RANBP2 contributes to human pathologies, and how the dynamic chromosomal region containingRANBP2 led to the appearance of theRGPD gene family during ape evolution. RANBP2/Nup358 (Ran Binding Protein 2) is a nucleoporin and a key component of the nuclear pore complex. Through its multiple functions (e.g. SUMOylation, regulation of nucleocytoplasmic transport) and subc...
Source: FEBS Letters - October 5, 2023 Category: Biochemistry Authors: Sophie Desgraupes,
Lucie Etienne,
Nathalie J. Arhel Tags: Review Source Type: research
Inhibiting SETD7 methyl ‐transferase activity impairs differentiation, lipid metabolism and lactogenesis in mammary epithelial cells
SETD7 (SET7/9, KMT7) is a lysine methyltransferase that regulates several pathways. In mammary epithelial cells (HC11 and EpH4), inhibiting SETD7 catalytic activity with the compound (R)-PFI2 increased cell proliferation, altered expression of E-cadherin, beta-catenin, lactoferrin, insulin-like growth factor binding protein 5, and beta-casein, and disrupted the lipid profile. These findings indicate that inhibiting SETD7 activity impairs mammary epithelial and lactogenic differentiation. SETD7 (SET7/9, KMT7) is a lysine methyltransferase that targets master regulators of cell proliferation and differentiation. Here, the im...
Source: FEBS Letters - October 4, 2023 Category: Biochemistry Authors: F átima Liliana Monteiro,
André Góis,
Inês Direito,
Tânia Melo,
Bruna Neves,
Mariana I. Alves,
Inês Batista,
Maria do Rosário Domingues,
Luisa A. Helguero Tags: Research Article Source Type: research
Evolutionary, structural and functional insights in nuclear organisation and nucleocytoplasmic transport in trypanosomes
We consider the features of the nuclear lamina and NPC comparing humans, yeasts and trypanosomes. We discuss how those nuclear elements are structured in trypanosomes and how they differ from, or are conserved with other eukaryotic lineages. We also discuss the functional and evolutionary aspects of those fundamental elements of nuclear structure. One of the remarkable features of eukaryotes is the nucleus, delimited by the nuclear envelope, a complex structure and home to the nuclear lamina and nuclear pore complex (NPC). For decades these structures were believed to be mainly architectural elements and, in the case of th...
Source: FEBS Letters - October 4, 2023 Category: Biochemistry Authors: Norma E. Padilla ‐Mejia,
Mark C. Field Tags: Review Source Type: research
The structure of a Lactobacillus helveticus chlorogenic acid esterase and the dynamics of its insertion domain provide insights into substrate binding
Chlorogenic acid esterases are biotechnologically useful enzymes that hydrolyze unwanted chlorogenic acid in foods, thereby improving their sensory properties. This work determines how two residues on hairpin loops above the active site influence substrate binding and turnover in a bacterial chlorogenic acid esterase. Chlorogenic acid esterases (ChlEs) are a useful class of enzymes that hydrolyze chlorogenic acid (CGA) into caffeic and quinic acids. ChlEs can break down CGA in foods to improve their sensory properties and release caffeic acid in the digestive system to improve the absorption of bioactive compounds. This wo...
Source: FEBS Letters - October 3, 2023 Category: Biochemistry Authors: Kellie K. Omori,
Charles T. Drucker,
Tracie L. S. Okumura,
Nathaniel B. Carl,
Brianna T. Dinn,
Destiny Ly,
Kylie N. Sacapano,
Allie Tajii,
Cedric P. Owens Tags: Research Article Source Type: research
