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Translational regulation of environmental adaptation in bacteria.
Tollerson, R, Ibba, M
The Journal of biological chemistry. 2020;(30):10434-10445
Abstract
Bacteria must rapidly respond to both intracellular and environmental changes to survive. One critical mechanism to rapidly detect and adapt to changes in environmental conditions is control of gene expression at the level of protein synthesis. At each of the three major steps of translation-initiation, elongation, and termination-cells use stimuli to tune translation rate and cellular protein concentrations. For example, changes in nutrient concentrations in the cell can lead to translational responses involving mechanisms such as dynamic folding of riboswitches during translation initiation or the synthesis of alarmones, which drastically alter cell physiology. Moreover, the cell can fine-tune the levels of specific protein products using programmed ribosome pausing or inducing frameshifting. Recent studies have improved understanding and revealed greater complexity regarding long-standing paradigms describing key regulatory steps of translation such as start-site selection and the coupling of transcription and translation. In this review, we describe how bacteria regulate their gene expression at the three translational steps and discuss how translation is used to detect and respond to changes in the cellular environment. Finally, we appraise the costs and benefits of regulation at the translational level in bacteria.
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Fluorine biocatalysis.
Wu, L, Maglangit, F, Deng, H
Current opinion in chemical biology. 2020;:119-126
Abstract
The introduction of fluorine atoms into organic molecules has received considerable attention as these organofluorines have often found widespread applications in bioorganic chemistry, medicinal chemistry and biomaterial science. Despite innovation of synthetic C-F forming methodologies, selective fluorination is still extremely challenging. Therefore, a biotransformation approach using fluorine biocatalysts is needed to selectively introduce fluorine into structurally diverse molecules. Yet, there are few ways that enable incorporation of fluorine into structurally complex bioactive molecules. One is to extend the substrate scope of the existing enzyme inventory. Another is to expand the biosynthetic pathways to accept fluorinated precursors for producing fluorinated bioactive molecules. Finally, an understanding of the physiological roles of fluorometabolites in the producing microorganisms will advance our ability to engineer a microorganism to produce novel fluorinated commodities. Here, we review the fluorinase biotechnology and fluorine biocatalysts that incorporate fluorine motifs to generate fluorinated molecules, and highlight areas for future developments.
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Two Distinct Photoprocesses in Cyanobacterial Bilin Pigments: Energy Migration in Light-Harvesting Phycobiliproteins versus Photoisomerization in Phytochromes.
Sineshchekov, VA, Bekasova, OD
Photochemistry and photobiology. 2020;(4):750-767
Abstract
The evolution of oxygenic photosynthesis, respiration and photoperception are connected with the appearance of cyanobacteria. The key compounds, which are involved in these processes, are tetrapyrroles: open chain - bilins and cyclic - chlorophylls and heme. The latter are characterized by their covalent bond with the apoprotein resulting in the formation of biliproteins. This type of photoreceptors is unique in that it can perform important and opposite functions-light-harvesting in photosynthesis with the participation of phycobiliproteins and photoperception mediated by phycochromes and phytochromes. In this review, cyanobacterial phycobiliproteins and phytochrome Cph1 are considered from a comparative point of view. Structural features of these pigments, which provide their contrasting photophysical and photochemical characteristics, are analyzed. The determining factor in the case of energy migration with the participation of phycobiliproteins is blocking the torsional relaxations of the chromophore, its D-ring, in the excited state and their freedom, in the case of phytochrome photoisomerization. From the energetics point of view, this distinction is preconditioned by the height of the activation barrier for the photoreaction and relaxation in the excited state, which depends on the degree of the chromophore fixation by its protein surroundings.
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4.
CRISPR/Cas Derivatives as Novel Gene Modulating Tools: Possibilities and In Vivo Applications.
Xu, X, Hulshoff, MS, Tan, X, Zeisberg, M, Zeisberg, EM
International journal of molecular sciences. 2020;(9)
Abstract
The field of genome editing started with the discovery of meganucleases (e.g., the LAGLIDADG family of homing endonucleases) in yeast. After the discovery of transcription activator-like effector nucleases and zinc finger nucleases, the recently discovered clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPR associated proteins (Cas) system has opened a new window of applications in the field of gene editing. Here, we review different Cas proteins and their corresponding features including advantages and disadvantages, and we provide an overview of the different endonuclease-deficient Cas protein (dCas) derivatives. These dCas derivatives consist of an endonuclease-deficient Cas9 which can be fused to different effector domains to perform distinct in vitro applications such as tracking, transcriptional activation and repression, as well as base editing. Finally, we review the in vivo applications of these dCas derivatives and discuss their potential to perform gene activation and repression in vivo, as well as their potential future use in human therapy.
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5.
Structure, Folding and Stability of Nucleoside Diphosphate Kinases.
Georgescauld, F, Song, Y, Dautant, A
International journal of molecular sciences. 2020;(18)
Abstract
Nucleoside diphosphate kinases (NDPK) are oligomeric proteins involved in the synthesis of nucleoside triphosphates. Their tridimensional structure has been solved by X-ray crystallography and shows that individual subunits present a conserved ferredoxin fold of about 140 residues in prokaryotes, archaea, eukaryotes and viruses. Monomers are functionally independent from each other inside NDPK complexes and the nucleoside kinase catalytic mechanism involves transient phosphorylation of the conserved catalytic histidine. To be active, monomers must assemble into conserved head to tail dimers, which further assemble into hexamers or tetramers. The interfaces between these oligomeric states are very different but, surprisingly, the assembly structure barely affects the catalytic efficiency of the enzyme. While it has been shown that assembly into hexamers induces full formation of the catalytic site and stabilizes the complex, it is unclear why assembly into tetramers is required for function. Several additional activities have been revealed for NDPK, especially in metastasis spreading, cytoskeleton dynamics, DNA binding and membrane remodeling. However, we still lack the high resolution structural data of NDPK in complex with different partners, which is necessary for deciphering the mechanism of these diverse functions. In this review we discuss advances in the structure, folding and stability of NDPKs.
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6.
Iron-sulfur cluster signaling: The common thread in fungal iron regulation.
Gupta, M, Outten, CE
Current opinion in chemical biology. 2020;:189-201
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Abstract
Iron homeostasis in fungi involves balancing iron uptake and storage with iron utilization to achieve adequate, nontoxic levels of this essential nutrient. Extensive work in the nonpathogenic yeast Saccharomyces cerevisiae and Schizosaccharomyces pombe has uncovered unique iron regulation networks for each organism that control iron metabolism via distinct molecular mechanisms. However, common themes have emerged from these studies. The activities of all fungal iron-sensing transcription factors characterized to date are regulated via iron-sulfur cluster signaling. Furthermore, glutaredoxins often play a key role in relaying the intracellular iron status to these DNA-binding proteins. Recent work with fungal pathogens, including Candida and Aspergillus species and Cryptococcus neoformans, has revealed novel iron regulation mechanisms, yet similar roles for iron-sulfur clusters and glutaredoxins in iron signaling have been confirmed. This review will focus on these recent discoveries regarding iron regulation pathways in both pathogenic and nonpathogenic fungi.
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7.
Making the Case for Disordered Proteins and Biomolecular Condensates in Bacteria.
Cohan, MC, Pappu, RV
Trends in biochemical sciences. 2020;(8):668-680
Abstract
Intrinsically disordered proteins/regions (IDPs/IDRs) contribute to a diverse array of molecular functions in eukaryotic systems. There is also growing recognition that membraneless biomolecular condensates, many of which are organized or regulated by IDPs/IDRs, can enable spatial and temporal regulation of complex biochemical reactions in eukaryotes. Motivated by these findings, we assess if (and how) membraneless biomolecular condensates and IDPs/IDRs are functionally involved in key cellular processes and molecular functions in bacteria. We summarize the conceptual underpinnings of condensate assembly and leverage these concepts by connecting them to recent findings that implicate specific types of condensates and IDPs/IDRs in important cellular level processes and molecular functions in bacterial systems.
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8.
Mechanisms for Induction of Microbial Extracellular Proteases in Response to Exterior Proteins.
Zhang, YZ, Zhang, WX, Chen, XL
Applied and environmental microbiology. 2020;(19)
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Abstract
Proteins are a main organic nitrogen source for microorganisms. Many heterotrophic microorganisms secrete extracellular proteases (ex-proteases) to efficiently decompose proteins into oligopeptides and amino acids when exterior proteins are required for growth. These ex-proteases not only play important roles in microbial nutrient acquisition or host infection but also contribute greatly to the global recycling of carbon and nitrogen. Moreover, may microbial ex-proteases have important applications in industrial, medical, and biotechnological areas. Therefore, uncovering the mechanisms by which microorganisms initiate the expression of ex-protease genes in response to exterior proteins is of great significance. In this review, the progress made in understanding the induction mechanisms of microbial ex-proteases in response to exterior proteins is summarized, with a focus on the inducer molecules, membrane sensors, and downstream pathways. Problems to be solved for better understanding of the induction mechanisms of microbial ex-proteases are also discussed.
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Quorum Sensing Circuits in the Communicating Mechanisms of Bacteria and Its Implication in the Biosynthesis of Bacteriocins by Lactic Acid Bacteria: a Review.
Kareb, O, Aïder, M
Probiotics and antimicrobial proteins. 2020;(1):5-17
Abstract
It is well established that bacteria communicate between each other by using different mechanisms; among which, quorum sensing (QS) is the best known one. Indeed, intra- and intercellular communications of microorganisms, as well as the regulation of metabolism and reaction to the surrounding environmental conditions, are carried out by using different signaling molecules. N-Acyl homoserine lactones control the QS in Gram-negative bacteria, while Gram-positive bacteria use communicating peptides. These compounds, by diffusing through the bacterial membrane cell from the extracellular medium, directly or indirectly control the expression of specific genes that induce bacteria to react to their surrounding environment and stressing agents. In the case of lactic acid bacteria and bifidobacteria which are widely used in the dairy industry, QS is of extreme importance for their survival and the extent of their activity in the dairy matrix. Moreover, it is also via QS that these bacteria synthesize various antimicrobial agents such as bacteriocins. The aim of this review is to highlight the quorum sensing circuits involved in the communicating mechanisms of bacteria with emphasis on current applications of QS in lactic acid bacteria. More particularly, the implication of QS in the biosynthesis of bacteriocins by lactic acid bacteria will be detailed.
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Carotenogenesis in cyanobacteria: CruA/CruP-type and CrtL-type lycopene cyclases.
Sugiyama, K, Takaichi, S
The Journal of general and applied microbiology. 2020;(2):53-58
Abstract
Cyanobacteria are oxygenic photoautotrophic prokaryotes containing chlorophylls and carotenoids, and the latter play important roles in light-harvesting, protection of excess light, assembly of pigment-protein complexes, and stabilization of lipid membranes. Cyanobacteria produce many kinds of carotenoids, such as β-carotene, zeaxanthin, echinenone, and myxol glycosides, which have a cyclic structure at one or both end(s). Cyclization of lycopene is a branch point in carotenoid biosynthesis to β-carotene and γ-carotene. Two types of lycopene cyclases, CruA/CruP-type and CrtL-type, are functionally confirmed in only five species, while homologous genes are found in the genomes of most cyanobacteria. This review summarizes the carotenogenesis pathways and the functional enzymes along with genes, focusing particularly on the cyclization of lycopene by distinct types of lycopene cyclases in cyanobacteria.