“…ALP, being a promiscuous ectoenzyme on the cell membrane, can enable the ENS of a wide range of substrates for many innovative applications, such as the patching of lipid rafts, as reported by Zhang et al 444 As shown in Figure 69, the authors used the metal complex Ru(II)(bpy) 3 as a threedimensional (3D) core to conjugate with the D-phosphotetrapeptide (Nap-ffk p y 263 ) to generate a metal complex (186) as the substrate of ALP. The authors, after confirming that ALP converted the solution of 186 to a hydrogel, incubated 186 with HeLa, HS-5, Ect1/E6E7, and A375 cells.…”
Section: Peri/intracellular Ensmentioning
confidence: 99%
“…Recent advances suggest that many enzymes act within NSs to facilitate the regulation of gene expression. , The best known molecular mechanism of nuclear speckle localization is a phosphorylation/dephosphorylation cycle of the arginine/serine repeat (RS) domain of serine rich (SR) proteins. Although it is generally believed that RS domain phosphorylation drives SR proteins from NSs to the nucleoplasm, a recent study reveals that synergistic interplay between PP1 and two splicing kinases (SRPK1 and CLK1) regulate the location of SR proteins, such as SRSF1 . Adams et al reported that SRSF1 binds to PP1 through the RRM1 domain and represses the catalytic activity of PP1 through an allosteric mechanism.…”
Section: Enzymatic
Noncovalent Synthesis In Naturementioning
Enzymatic reactions and noncovalent (i.e., supramolecular) interactions are two fundamental nongenetic attributes of life. Enzymatic noncovalent synthesis (ENS) refers to a process where enzymatic reactions control intermolecular noncovalent interactions for spatial organization of higher-order molecular assemblies that exhibit emergent properties and functions. Like enzymatic covalent synthesis (ECS), in which an enzyme catalyzes the formation of covalent bonds to generate individual molecules, ENS is a unifying theme for understanding the functions, morphologies, and locations of molecular ensembles in cellular environments. This review intends to provide a summary of the works of ENS within the last decade and emphasize ENS for functions. After comparing ECS and ENS, we describe a few representative examples where nature uses ENS, as a rule of life, to create the ensembles of biomacromolecules for emergent properties/functions in a myriad of cellular processes. Then, we focus on ENS of man-made (synthetic) molecules in cell-free conditions, classified by the types of enzymes. After that, we introduce the exploration of ENS of man-made molecules in the context of cells by discussing intercellular, peri/intracellular, and subcellular ENS for cell morphogenesis, molecular imaging, cancer therapy, and other applications. Finally, we provide a perspective on the promises of ENS for developing molecular assemblies/processes for functions. This review aims to be an updated introduction for researchers who are interested in exploring noncovalent synthesis for developing molecular science and technologies to address societal needs.
“…ALP, being a promiscuous ectoenzyme on the cell membrane, can enable the ENS of a wide range of substrates for many innovative applications, such as the patching of lipid rafts, as reported by Zhang et al 444 As shown in Figure 69, the authors used the metal complex Ru(II)(bpy) 3 as a threedimensional (3D) core to conjugate with the D-phosphotetrapeptide (Nap-ffk p y 263 ) to generate a metal complex (186) as the substrate of ALP. The authors, after confirming that ALP converted the solution of 186 to a hydrogel, incubated 186 with HeLa, HS-5, Ect1/E6E7, and A375 cells.…”
Section: Peri/intracellular Ensmentioning
confidence: 99%
“…Recent advances suggest that many enzymes act within NSs to facilitate the regulation of gene expression. , The best known molecular mechanism of nuclear speckle localization is a phosphorylation/dephosphorylation cycle of the arginine/serine repeat (RS) domain of serine rich (SR) proteins. Although it is generally believed that RS domain phosphorylation drives SR proteins from NSs to the nucleoplasm, a recent study reveals that synergistic interplay between PP1 and two splicing kinases (SRPK1 and CLK1) regulate the location of SR proteins, such as SRSF1 . Adams et al reported that SRSF1 binds to PP1 through the RRM1 domain and represses the catalytic activity of PP1 through an allosteric mechanism.…”
Section: Enzymatic
Noncovalent Synthesis In Naturementioning
Enzymatic reactions and noncovalent (i.e., supramolecular) interactions are two fundamental nongenetic attributes of life. Enzymatic noncovalent synthesis (ENS) refers to a process where enzymatic reactions control intermolecular noncovalent interactions for spatial organization of higher-order molecular assemblies that exhibit emergent properties and functions. Like enzymatic covalent synthesis (ECS), in which an enzyme catalyzes the formation of covalent bonds to generate individual molecules, ENS is a unifying theme for understanding the functions, morphologies, and locations of molecular ensembles in cellular environments. This review intends to provide a summary of the works of ENS within the last decade and emphasize ENS for functions. After comparing ECS and ENS, we describe a few representative examples where nature uses ENS, as a rule of life, to create the ensembles of biomacromolecules for emergent properties/functions in a myriad of cellular processes. Then, we focus on ENS of man-made (synthetic) molecules in cell-free conditions, classified by the types of enzymes. After that, we introduce the exploration of ENS of man-made molecules in the context of cells by discussing intercellular, peri/intracellular, and subcellular ENS for cell morphogenesis, molecular imaging, cancer therapy, and other applications. Finally, we provide a perspective on the promises of ENS for developing molecular assemblies/processes for functions. This review aims to be an updated introduction for researchers who are interested in exploring noncovalent synthesis for developing molecular science and technologies to address societal needs.
“…NB are made up of RNA and proteins, and hold their structure by the interactions existing between them: RNA-protein or protein-protein. These proteins are constantly exchanged with the nucleoplasm regulated by post-translational modifications like phosphorylation and SUMOylation [38], there being proteins common to different NB and others specific of a certain type of NB [3,29,39,47; https://www.ebi.ac.uk/QuickGO/term/]. With respect to the formation of NB, three models are considered: The first is the model of stochastic assembly where the components of the NB are grouped without a defined order; the assembly is random.…”
Section: Introductionmentioning
confidence: 99%
“…Nuclear bodies. It's shown the percentages in which the different nuclear bodies were mentioned in the selected articles[1,5,7,9,11,12,17,20,23,24,26,29,30,32,33,35,36,39,42,43,45,47,51,52,53,55] …”
Background: Nuclear bodies (NB) are membrane-less subnuclear organelles that perform important functions in the cell, such as transcription, RNA splicing, processing and transport of ribosomal pre-RNA, epigenetic regulation, and others. The aim of the work was to analyse the classification of NB in the Terminologia Histologica (TH) and biological and bibliographical databases. Materials and methods: The semantic structure of the Nucleoplasm section in the TH was analysed and unsystematic bibliographical search was made in the PubMed, SciELO, EMBASE databases and European Bioinformatics Institute (EMBL-EBI) biology database to identify which structures are classified as NB. Results: It was found that the terms Corpusculum convolutum, Macula interchromatinea and Corpusculum PML are not correctly classified in the TH, since they are subordinated under the term Chromatinum and not under Corpusculum nucleare. The bibliography consulted showed that 100%, 92.6% and 81.5% of articles mentioned Corpusculum convolutum, Macula interchromatinea and Corpusculum PML, respectively as nuclear bodies. Conclusions: It is suggested to relocate the terms Corpusculum convolutum, Macula interchromatinea and Corpusculum PML with the name of Corpusculum nucleare and the incorporation of two new entities to the Histological Terminology according to the information collected: paraspeckles and histone locus body.
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