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1.
Biophys J ; 123(11): 1508-1518, 2024 Jun 04.
Artículo en Inglés | MEDLINE | ID: mdl-38664966

RESUMEN

Biomolecular condensates have emerged as a powerful new paradigm in cell biology with broad implications to human health and disease, particularly in the nucleus where phase separation is thought to underly elements of chromatin organization and regulation. Specifically, it has been recently reported that phase separation of heterochromatin protein 1alpha (HP1α) with DNA contributes to the formation of condensed chromatin states. HP1α localization to heterochromatic regions is mediated by its binding to specific repressive marks on the tail of histone H3, such as trimethylated lysine 9 on histone H3 (H3K9me3). However, whether epigenetic marks play an active role in modulating the material properties of HP1α and dictating emergent functions of its condensates remains to be understood. Here, we leverage a reductionist system, composed of modified and unmodified histone H3 peptides, HP1α, and DNA, to examine the contribution of specific epigenetic marks to phase behavior of HP1α. We show that the presence of histone peptides bearing the repressive H3K9me3 is compatible with HP1α condensates, whereas peptides containing unmodified residues or bearing the transcriptional activation mark H3K4me3 are incompatible with HP1α phase separation. Using fluorescence microscopy and rheological approaches, we further demonstrate that H3K9me3 histone peptides modulate the dynamics and viscoelastic network properties of HP1α condensates in a concentration-dependent manner. Additionally, in cells exposed to uniaxial strain, we find there to be a decreased ratio of nuclear H3K9me3 to HP1α. These data suggest that HP1α-DNA condensates are viscoelastic materials, whose properties may provide an explanation for the dynamic behavior of heterochromatin in cells and in response to mechanostimulation.


Asunto(s)
Homólogo de la Proteína Chromobox 5 , Proteínas Cromosómicas no Histona , Epigénesis Genética , Histonas , Proteínas Cromosómicas no Histona/metabolismo , Proteínas Cromosómicas no Histona/química , Histonas/metabolismo , Histonas/química , Humanos , ADN/metabolismo , ADN/química , Condensados Biomoleculares/metabolismo , Condensados Biomoleculares/química
2.
bioRxiv ; 2024 Feb 09.
Artículo en Inglés | MEDLINE | ID: mdl-38370661

RESUMEN

Biomolecular condensates have emerged as a powerful new paradigm in cell biology with broad implications to human health and disease, particularly in the nucleus where phase separation is thought to underly elements of chromatin organization and regulation. Specifically, it has been recently reported that phase separation of heterochromatin protein 1alpha (HP1α) with DNA contributes to the formation of condensed chromatin states. HP1α localization to heterochromatic regions is mediated by its binding to specific repressive marks on the tail of histone H3, such as trimethylated lysine 9 on histone H3 (H3K9me3). However, whether epigenetic marks play an active role in modulating the material properties of HP1α and dictating emergent functions of its condensates, remains only partially understood. Here, we leverage a reductionist system, comprised of modified and unmodified histone H3 peptides, HP1α and DNA to examine the contribution of specific epigenetic marks to phase behavior of HP1α. We show that the presence of histone peptides bearing the repressive H3K9me3 is compatible with HP1α condensates, while peptides containing unmodified residues or bearing the transcriptional activation mark H3K4me3 are incompatible with HP1α phase separation. In addition, inspired by the decreased ratio of nuclear H3K9me3 to HP1α detected in cells exposed to uniaxial strain, using fluorescence microscopy and rheological approaches we demonstrate that H3K9me3 histone peptides modulate the dynamics and network properties of HP1α condensates in a concentration dependent manner. These data suggest that HP1α-DNA condensates are viscoelastic materials, whose properties may provide an explanation for the dynamic behavior of heterochromatin in cells in response to mechanostimulation.

3.
Commun Chem ; 7(1): 49, 2024 Feb 29.
Artículo en Inglés | MEDLINE | ID: mdl-38424154

RESUMEN

Peptide-based liquid-liquid phase separated domains, or coacervates, are a biomaterial gaining new interest due to their exciting potential in fields ranging from biosensing to drug delivery. In this study, we demonstrate that coacervates provide a simple and biocompatible medium to improve nucleic acid biosensors through the sequestration of both the biosensor and target strands within the coacervate, thereby increasing their local concentration. Using the well-established polyarginine (R9) - ATP coacervate system and an energy transfer-based DNA molecular beacon we observed three key improvements: i) a greater than 20-fold reduction of the limit of detection within coacervates when compared to control buffer solutions; ii) an increase in the kinetics, equilibrium was reached more than 4-times faster in coacervates; and iii) enhancement in the dye fluorescent quantum yields within the coacervates, resulting in greater signal-to-noise. The observed benefits translate into coacervates greatly improving bioassay functionality.

4.
Angew Chem Int Ed Engl ; 62(50): e202311479, 2023 12 11.
Artículo en Inglés | MEDLINE | ID: mdl-37934145

RESUMEN

A conceptual framework towards understanding biological condensed phases is emerging, derived from biological, biomimetic, and synthetic sequences. However, de novo peptide condensate design remains a challenge due to an incomplete understanding of the structural and interactive complexity. We designed peptide modules based on a simple repeat motif composed of tripeptide spacers (GSG, SGS, GLG) interspersed with adhesive amino acids (R/H and Y). We show, using sequence editing and a combination of computation and experiment, that n→π* interactions in GLG backbones are a dominant factor in providing sufficient backbone structure, which in turn regulates the water interface, collectively promoting liquid droplet formation. Moreover, these R(GLG)Y and H(GLG)Y condensates unexpectedly display sequence-dependent emission that is a consequence of their non-covalent network interactions, and readily observable by confocal microscopy.


Asunto(s)
Aminoácidos , Péptidos , Fluorescencia , Péptidos/química , Aminoácidos/química
5.
Chem Commun (Camb) ; 59(95): 14138-14141, 2023 Nov 28.
Artículo en Inglés | MEDLINE | ID: mdl-37955166

RESUMEN

Melanin pigments are found in most life forms, where they are responsible for coloration and ultraviolet (UV) light protection. Natural melanin is a poorly soluble and complex biosynthesis product produced through confined and templated enzymatic oxidation of tyrosine. It has been challenging to create water-soluble synthetic mimics. This study demonstrates the enzymatic synthesis of oxidized phenols confined inside liquid droplets. We use an amphiphilic, bifunctional peptide, DYFR9, that combines a tyrosine tripeptide previously shown to undergo enzymatic oxidation to form peptide pigments with broad absorbance, and polyarginine to facilitate complex coacervation in the presence of ATP. When ATP, DYFR9 are mixed and exposed to tyrosinase, pigmented liquid droplets result, while no appreciable oxidation is observed in the bulk.


Asunto(s)
Melaninas , Tirosina , Monofenol Monooxigenasa , Péptidos , Adenosina Trifosfato
6.
J Mol Biol ; 435(5): 167971, 2023 03 01.
Artículo en Inglés | MEDLINE | ID: mdl-36690068

RESUMEN

In the past almost 15 years, we witnessed the birth of a new scientific field focused on the existence, formation, biological functions, and disease associations of membraneless bodies in cells, now referred to as biomolecular condensates. Pioneering studies from several laboratories [reviewed in1-3] supported a model wherein biomolecular condensates associated with diverse biological processes form through the process of phase separation. These and other findings that followed have revolutionized our understanding of how biomolecules are organized in space and time within cells to perform myriad biological functions, including cell fate determination, signal transduction, endocytosis, regulation of gene expression and protein translation, and regulation of RNA metabolism. Further, condensates formed through aberrant phase transitions have been associated with numerous human diseases, prominently including neurodegeneration and cancer. While in some cases, rigorous evidence supports links between formation of biomolecular condensates through phase separation and biological functions, in many others such links are less robustly supported, which has led to rightful scrutiny of the generality of the roles of phase separation in biology and disease.4-7 During a week-long workshop in March 2022 at the Telluride Science Research Center (TSRC) in Telluride, Colorado, ∼25 scientists addressed key questions surrounding the biomolecular condensates field. Herein, we present insights gained through these discussions, addressing topics including, roles of condensates in diverse biological processes and systems, and normal and disease cell states, their applications to synthetic biology, and the potential for therapeutically targeting biomolecular condensates.


Asunto(s)
Condensados Biomoleculares , Enfermedad , Transición de Fase , Humanos
7.
Chem Sci ; 13(48): 14346-14356, 2022 Dec 14.
Artículo en Inglés | MEDLINE | ID: mdl-36545145

RESUMEN

Proteins are an important class of biologics, but there are several recurring challenges to address when designing protein-based therapeutics. These challenges include: the propensity of proteins to aggregate during formulation, relatively low loading in traditional hydrophobic delivery vehicles, and inefficient cellular uptake. This last criterion is particularly challenging for anionic proteins as they cannot cross the anionic plasma membrane. Here we investigated the complex coacervation of anionic proteins with a block copolymer of opposite charge to form polyelectrolyte complex (PEC) micelles for use as a protein delivery vehicle. Using genetically modified variants of the model protein green fluorescent protein (GFP), we evaluated the role of protein charge and charge localization in the formation and stability of PEC micelles. A neutral-cationic block copolymer, poly(oligoethylene glycol methacrylate-block-quaternized 4-vinylpyridine), POEGMA79-b-qP4VP175, was prepared via RAFT polymerization for complexation and microphase separation with the panel of engineered anionic GFPs. We found that isotropically supercharged proteins formed micelles at higher ionic strength relative to protein variants with charge localized to a polypeptide tag. We then studied GFP delivery by PEC micelles and found that they effectively delivered the protein cargo to mammalian cells. However, cellular delivery varied as a function of protein charge and charge distribution and we found an inverse relationship between the PEC micelle critical salt concentration and delivery efficiency. This model system has highlighted the potential of polyelectrolyte complexes to deliver anionic proteins intracellularly. Using this model system, we have identified requirements for the formation of PEC micelles that are stable at physiological ionic strength and that smaller protein-polyelectrolyte complexes effectively deliver proteins to Jurkat cells.

8.
Proc Natl Acad Sci U S A ; 119(37): e2202240119, 2022 09 13.
Artículo en Inglés | MEDLINE | ID: mdl-36067308

RESUMEN

Liquid-liquid phase separation of tropoelastin has long been considered to be an important early step in the complex process of elastin fiber assembly in the body and has inspired the development of elastin-like peptides with a wide range of industrial and biomedical applications. Despite decades of study, the material state of the condensed liquid phase of elastin and its subsequent maturation remain poorly understood. Here, using a model minielastin that mimics the alternating domain structure of full-length tropoelastin, we examine the elastin liquid phase. We combine differential interference contrast (DIC), fluorescence, and scanning electron microscopy with particle-tracking microrheology to resolve the material transition occurring within elastin liquids over time in the absence of exogenous cross-linking. We find that this transition is accompanied by an intermediate stage marked by the coexistence of insoluble solid and dynamic liquid phases giving rise to significant spatial heterogeneities in material properties. We further demonstrate that varying the length of the terminal hydrophobic domains of minielastins can tune the maturation process. This work not only resolves an important step in the hierarchical assembly process of elastogenesis but further contributes mechanistic insight into the diverse repertoire of protein condensate maturation pathways with emerging importance across biology.


Asunto(s)
Elastina , Tropoelastina , Elastina/química , Interacciones Hidrofóbicas e Hidrofílicas , Péptidos/química , Tropoelastina/metabolismo
9.
J Am Chem Soc ; 144(33): 15002-15007, 2022 08 24.
Artículo en Inglés | MEDLINE | ID: mdl-35946870

RESUMEN

Supramolecular self-assembly of fibrous components and liquid-liquid phase separation are at the extremes of the order-to-disorder spectrum. They collectively play key roles in cellular organization. It is still a major challenge to design systems where both highly ordered nanostructures and liquid-liquid phase-separated domains can coexist. We present a three-component assembly approach that generates fibrous domains that exclusively form inside globally disordered, liquid condensates. This is achieved by creating amphiphilic peptides that combine the features of fibrillar assembly (the amyloid domain LVFFA) and complex coacervation (oligo-arginine and adenosine triphosphate (ATP)) in one peptide, namely, LVFFAR9. When this hybrid peptide is mixed in different ratios with R9 and ATP, we find that conditions can be created where fibrous assembly is exclusively observed inside liquid coacervates. Through fluorescence and atomic force microscopy characterization, we investigate the dynamic evolution of ordered and disordered features over time. It was observed that the fibers nucleate and mature inside the droplets and that these fiber-containing liquid droplets can also undergo fusion, showing that the droplets remain liquid-like. Our work thus generates opportunities for the design of ordered structures within the confined environment of biomolecular condensates, which may be useful to create supramolecular materials in defined compartments and as model systems that can enhance understanding of ordering principles in biology.


Asunto(s)
Nanoestructuras , Péptidos , Adenosina Trifosfato , Amiloide , Proteínas Amiloidogénicas , Nanoestructuras/química
10.
Protein Sci ; 30(7): 1482-1486, 2021 07.
Artículo en Inglés | MEDLINE | ID: mdl-33966305

RESUMEN

Huntington's disease is caused by a polyglutamine (polyQ) expansion in the huntingtin protein which results in its abnormal aggregation in the nervous system. Huntingtin aggregates are linked to toxicity and neuronal dysfunction, but a comprehensive understanding of the aggregation mechanism in vivo remains elusive. Here, we examine the morphology of polyQ aggregates in Caenorhabditis elegans mechanosensory neurons as a function of age using confocal and fluorescence lifetime imaging microscopy. We find that aggregates in young worms are mostly spherical with homogenous intensity, but as the worm ages aggregates become substantially more heterogeneous. Most prominently, in older worms we observe an apparent core/shell morphology of polyQ assemblies with decreased intensity in the center. The fluorescence lifetime of polyQ is uniform across the aggregate indicating that the dimmed intensity in the assembly center is most likely not due to quenching or changes in local environment, but rather to displacement of fluorescent polyQ from the central region. This apparent core/shell architecture of polyQ aggregates in aging C. elegans neurons contributes to the diverse landscape of polyQ aggregation states implicated in Huntington's disease.


Asunto(s)
Envejecimiento/metabolismo , Proteínas de Caenorhabditis elegans/metabolismo , Caenorhabditis elegans/metabolismo , Mecanorreceptores/metabolismo , Péptidos/metabolismo , Agregado de Proteínas , Envejecimiento/genética , Animales , Caenorhabditis elegans/genética , Proteínas de Caenorhabditis elegans/genética , Péptidos/genética
12.
Nat Commun ; 11(1): 4628, 2020 09 15.
Artículo en Inglés | MEDLINE | ID: mdl-32934220

RESUMEN

Liquid phase separation into two or more coexisting phases has emerged as a new paradigm for understanding subcellular organization, prebiotic life, and the origins of disease. The design principles underlying biomolecular phase separation have the potential to drive the development of novel liquid-based organelles and therapeutics, however, an understanding of how individual molecules contribute to emergent material properties, and approaches to directly manipulate phase dynamics are lacking. Here, using microrheology, we demonstrate that droplets of poly-arginine coassembled with mono/polynucleotides have approximately 100 fold greater viscosity than comparable lysine droplets, both of which can be finer tuned by polymer length. We find that these amino acid-level differences can drive the formation of coexisting immiscible phases with tunable formation kinetics and can be further exploited to trigger the controlled release of droplet components. Together, this work provides a novel mechanism for leveraging sequence-level components in order to regulate droplet dynamics and multiphase coexistence.


Asunto(s)
Arginina/química , Lisina/química , Cinética , Transición de Fase , Polinucleótidos/química , Viscosidad
13.
J Biol Chem ; 294(18): 7160-7168, 2019 05 03.
Artículo en Inglés | MEDLINE | ID: mdl-30914480

RESUMEN

Phase separation of biomolecules leading to the formation of assemblies with distinct material properties has recently emerged as a new paradigm underlying subcellular organization. The discovery that disordered proteins, long associated with aggregation in neurodegenerative disease, are also implicated in driving liquid phase separation has galvanized significant interest in exploring the relationship between misregulated phase transitions and disease. This review summarizes recent work linking liquid phase separation to neurodegeneration, highlighting a pathological role for altered phase behavior and material properties of proteins assembled via liquid phase separation. The techniques that recent and current work in this area have deployed are also discussed, as is the potential for these discoveries to promote new research directions for investigating the molecular etiologies of neurodegenerative diseases.


Asunto(s)
Enfermedades Neurodegenerativas/metabolismo , Transición de Fase , Humanos , Simulación de Dinámica Molecular , Proteínas/metabolismo
14.
Methods Enzymol ; 611: 31-50, 2018.
Artículo en Inglés | MEDLINE | ID: mdl-30471691

RESUMEN

Phase separation has emerged as a new paradigm currently revolutionizing our understanding of cell biology and intracellular organization. Disordered protein domains have recently been demonstrated as integral drivers of phase separation into condensed liquids with emergent material properties. Using in vitro model systems employing purified protein components is necessary to interrogate the molecular mechanisms underlying phase separation; however, these systems pose many experimental challenges. In this chapter we describe general strategies for purifying, handling, imaging, and characterizing the phase behavior of disordered proteins. We further outline methods for the purification of the model P granule protein LAF-1, the construction of phase diagrams, and the quantification of liquid droplet fusion or coalescence.


Asunto(s)
Proteínas Intrínsecamente Desordenadas/química , Microscopía/métodos , Transición de Fase , Animales , Caenorhabditis elegans/química , Proteínas de Caenorhabditis elegans/química , Gránulos Citoplasmáticos/química , Diseño de Equipo , Proteínas Intrínsecamente Desordenadas/aislamiento & purificación , Microscopía/instrumentación , Concentración Osmolar , ARN Helicasas/química
15.
Nat Chem ; 9(11): 1118-1125, 2017 11.
Artículo en Inglés | MEDLINE | ID: mdl-29064502

RESUMEN

Many intracellular membraneless organelles form via phase separation of intrinsically disordered proteins (IDPs) or regions (IDRs). These include the Caenorhabditis elegans protein LAF-1, which forms P granule-like droplets in vitro. However, the role of protein disorder in phase separation and the macromolecular organization within droplets remain elusive. Here, we utilize a novel technique, ultrafast-scanning fluorescence correlation spectroscopy, to measure the molecular interactions and full coexistence curves (binodals), which quantify the protein concentration within LAF-1 droplets. The binodals of LAF-1 and its IDR display a number of unusual features, including 'high concentration' binodal arms that correspond to remarkably dilute droplets. We find that LAF-1 and other in vitro and intracellular droplets are characterized by an effective mesh size of ∼3-8 nm, which determines the size scale at which droplet properties impact molecular diffusion and permeability. These findings reveal how specific IDPs can phase separate to form permeable, low-density (semi-dilute) liquids, whose structural features are likely to strongly impact biological function.


Asunto(s)
Proteínas Intrínsecamente Desordenadas/química , Orgánulos/química , Simulación de Dinámica Molecular , Método de Montecarlo , Tamaño de la Partícula , Permeabilidad , Espectrometría de Fluorescencia
16.
Methods Cell Biol ; 141: 27-44, 2017.
Artículo en Inglés | MEDLINE | ID: mdl-28882307

RESUMEN

Fluorescence correlation spectroscopy and single-molecule Förster resonance energy transfer are powerful and versatile techniques to quantify and describe molecular interactions. They are particularly well suited to the study of dynamic proteins and assemblies, as they can overcome some of the challenges that stymie more conventional ensemble approaches. In this chapter, we describe the application of these methods to study the interaction of tau with the molecular aggregation inducer, heparin, and the functional binding partner, soluble tubulin. Specifically, we outline the practical aspects of both techniques to characterize the critical first steps of tau aggregation and tau-mediated microtubule polymerization. The information gained from these measurements provides unique insight into tau function and its role in disease.


Asunto(s)
Transferencia Resonante de Energía de Fluorescencia/métodos , Heparina/metabolismo , Espectrometría de Fluorescencia/métodos , Tubulina (Proteína)/metabolismo , Proteínas tau/metabolismo , Sitios de Unión , Fluorescencia , Humanos , Modelos Moleculares , Complejos Multiproteicos , Unión Proteica , Conformación Proteica , Imagen Individual de Molécula , Proteínas tau/química
17.
Proc Natl Acad Sci U S A ; 113(50): 14336-14341, 2016 12 13.
Artículo en Inglés | MEDLINE | ID: mdl-27911791

RESUMEN

Tau is an intrinsically disordered protein with an important role in maintaining the dynamic instability of neuronal microtubules. Despite intensive study, a detailed understanding of the functional mechanism of tau is lacking. Here, we address this deficiency by using intramolecular single-molecule Förster Resonance Energy Transfer (smFRET) to characterize the conformational ensemble of tau bound to soluble tubulin heterodimers. Tau adopts an open conformation on binding tubulin, in which the long-range contacts between both termini and the microtubule binding region that characterize its compact solution structure are diminished. Moreover, the individual repeats within the microtubule binding region that directly interface with tubulin expand to accommodate tubulin binding, despite a lack of extension in the overall dimensions of this region. These results suggest that the disordered nature of tau provides the significant flexibility required to allow for local changes in conformation while preserving global features. The tubulin-associated conformational ensemble is distinct from its aggregation-prone one, highlighting differences between functional and dysfunctional states of tau. Using constraints derived from our measurements, we construct a model of tubulin-bound tau, which draws attention to the importance of the role of tau's conformational plasticity in function.


Asunto(s)
Proteínas Intrínsecamente Desordenadas/química , Proteínas Intrínsecamente Desordenadas/metabolismo , Tubulina (Proteína)/química , Tubulina (Proteína)/metabolismo , Proteínas tau/química , Proteínas tau/metabolismo , Animales , Sitios de Unión , Transferencia Resonante de Energía de Fluorescencia , Humanos , Cinética , Microtúbulos/metabolismo , Modelos Moleculares , Complejos Multiproteicos/química , Complejos Multiproteicos/metabolismo , Neuronas/metabolismo , Unión Proteica , Dominios y Motivos de Interacción de Proteínas , Multimerización de Proteína
18.
Soft Matter ; 12(45): 9142-9150, 2016 Nov 16.
Artículo en Inglés | MEDLINE | ID: mdl-27791212

RESUMEN

Living cells contain numerous membrane-less RNA/protein (RNP) bodies that assemble by intracellular liquid-liquid phase separation. The properties of these condensed phase droplets are increasingly recognized as important in their physiological function within living cells, and also through the link to protein aggregation pathologies. However, techniques such as droplet coalescence analysis or standard microrheology do not always enable robust property measurements of model RNA/protein droplets in vitro. Here, we introduce a microfluidic platform that drives protein droplets into a single large phase, which facilitates viscosity measurements using passive microrheology and/or active two-phase flow analysis. We use this technique to study various phase separating proteins from structures including P granules, nucleoli, and Whi3 droplets. In each case, droplets exhibit simple liquid behavior, with shear rate-independent viscosities, over observed timescales. Interestingly, we find that a reported order of magnitude difference between the timescale of Whi3 and LAF-1 droplet coalescence is driven by large differences in surface tension rather than viscosity, with implications for droplet assembly and function. The ability to simultaneously perform active and passive microrheological measurements enables studying the impact of ATP-dependent biological activity on RNP droplets, which is a key area for future research.


Asunto(s)
Microfluídica , Orgánulos/química , Proteínas/química , ARN/química , Tensión Superficial , Viscosidad
19.
Dev Cell ; 35(5): 531-532, 2015 Dec 07.
Artículo en Inglés | MEDLINE | ID: mdl-26651288

RESUMEN

Recent advances suggest that phase transitions of proteins into liquid or hydrogel states could underlie pathological protein aggregation associated with neurodegenerative disease. In a recent issue of Neuron, Murakami et al. (2015) demonstrate that ALS-associated FUS mutations abrogate the reversibility of condensed liquids and/or hydrogels, leading to neurotoxicity in C. elegans.


Asunto(s)
Esclerosis Amiotrófica Lateral/genética , Proteínas de Caenorhabditis elegans/genética , Degeneración Lobar Frontotemporal/genética , Hidrogeles , Actividad Motora/genética , Transición de Fase , ARN Mensajero/metabolismo , Proteína FUS de Unión a ARN/genética , Animales
20.
Mol Cell ; 60(2): 220-30, 2015 Oct 15.
Artículo en Inglés | MEDLINE | ID: mdl-26474065

RESUMEN

Compartmentalization in cells is central to the spatial and temporal control of biochemistry. In addition to membrane-bound organelles, membrane-less compartments form partitions in cells. Increasing evidence suggests that these compartments assemble through liquid-liquid phase separation. However, the spatiotemporal control of their assembly, and how they maintain distinct functional and physical identities, is poorly understood. We have previously shown an RNA-binding protein with a polyQ-expansion called Whi3 is essential for the spatial patterning of cyclin and formin transcripts in cytosol. Here, we show that specific mRNAs that are known physiological targets of Whi3 drive phase separation. mRNA can alter the viscosity of droplets, their propensity to fuse, and the exchange rates of components with bulk solution. Different mRNAs impart distinct biophysical properties of droplets, indicating mRNA can bring individuality to assemblies. Our findings suggest that mRNAs can encode not only genetic information but also the biophysical properties of phase-separated compartments.


Asunto(s)
Proteínas Fúngicas/metabolismo , Regulación Fúngica de la Expresión Génica , Péptidos/química , ARN de Hongos/metabolismo , ARN Mensajero/metabolismo , Proteínas de Unión al ARN/metabolismo , Saccharomycetales/metabolismo , Compartimento Celular , Ciclinas/química , Ciclinas/genética , Ciclinas/metabolismo , Escherichia coli/genética , Escherichia coli/metabolismo , Proteínas Fúngicas/química , Proteínas Fúngicas/genética , Expresión Génica , Proteínas de Microfilamentos/química , Proteínas de Microfilamentos/genética , Proteínas de Microfilamentos/metabolismo , Orgánulos/química , Orgánulos/metabolismo , Péptidos/metabolismo , Transición de Fase , Proteínas de Unión al ARN/química , Proteínas de Unión al ARN/genética , Proteínas Recombinantes de Fusión/química , Proteínas Recombinantes de Fusión/genética , Proteínas Recombinantes de Fusión/metabolismo , Reología , Saccharomycetales/química , Saccharomycetales/genética
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