Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 20 de 10.366
Filtrar
1.
Open Biol ; 13(1): 220238, 2023 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-36629021

RESUMO

The endobiotic flagellate Monocercomonoides exilis is the only known eukaryote to have lost mitochondria and all its associated proteins in its evolutionary past. This final stage of the mitochondrial evolutionary pathway may serve as a model to explain events at their very beginning such as the initiation of protein import. We have assessed the capability of proteins from this eukaryote to enter emerging mitochondria using a specifically designed in vitro assay. Hydrogenosomes (reduced mitochondria) of Trichomonas vaginalis were incubated with a soluble protein pool derived from a cytosolic fraction of M. exilis, and proteins entering hydrogenosomes were subsequently detected by mass spectrometry. The assay detected 19 specifically and reproducibly imported proteins, and in 14 cases the import was confirmed by the overexpression of their tagged version in T. vaginalis. In most cases, only a small portion of the signal reached the hydrogenosomes, suggesting specific but inefficient transport. Most of these proteins represent enzymes of carbon metabolism, and none exhibited clear signatures of proteins targeted to hydrogenosomes or mitochondria, which is consistent with their inefficient import. The observed phenomenon may resemble a primaeval type of protein import which might play a role in the establishment of the organelle and shaping of its proteome in the initial stages of endosymbiosis.


Assuntos
Eucariotos , Proteínas de Protozoários , Eucariotos/metabolismo , Proteínas de Protozoários/metabolismo , Organelas/química , Organelas/metabolismo , Mitocôndrias/metabolismo , Transporte Proteico
2.
Nat Commun ; 14(1): 421, 2023 Jan 26.
Artigo em Inglês | MEDLINE | ID: mdl-36702825

RESUMO

Inspired by the role of intracellular liquid-liquid phase separation (LLPS) in formation of membraneless organelles, there is great interest in developing dynamic compartments formed by LLPS of intrinsically disordered proteins (IDPs) or short peptides. However, the molecular mechanisms underlying the formation of biomolecular condensates have not been fully elucidated, rendering on-demand design of synthetic condensates with tailored physico-chemical functionalities a significant challenge. To address this need, here we design a library of LLPS-promoting peptide building blocks composed of various assembly domains. We show that the LLPS propensity, dynamics, and encapsulation efficiency of compartments can be tuned by changes to the peptide composition. Specifically, with the aid of Raman and NMR spectroscopy, we show that interactions between arginine and aromatic amino acids underlie droplet formation, and that both intra- and intermolecular interactions dictate droplet dynamics. The resulting sequence-structure-function correlation could support the future development of compartments for a variety of applications.


Assuntos
Condensados Biomoleculares , Proteínas Intrinsicamente Desordenadas , Aminoácidos Aromáticos , Espectroscopia de Ressonância Magnética , Peptídeos/análise , Proteínas Intrinsicamente Desordenadas/metabolismo , Organelas/metabolismo
3.
Int J Mol Sci ; 24(1)2023 Jan 03.
Artigo em Inglês | MEDLINE | ID: mdl-36614328

RESUMO

Mitochondria have been recognized as the energy (in the form of ATP)-producing cell organelles, required for cell viability, survival and normal cell function [...].


Assuntos
Mitocôndrias , Organelas , Mitocôndrias/metabolismo , Sobrevivência Celular , Dinâmica Mitocondrial , Metabolismo Energético
4.
Curr Biol ; 33(1): R22-R25, 2023 Jan 09.
Artigo em Inglês | MEDLINE | ID: mdl-36626858

RESUMO

Understanding the order and importance of events through which endosymbionts transition into cellular organelles (organellogenesis) is central to hypotheses about the origin of the eukaryotic cell. A new study on host-symbiont integration in a unicellular eukaryote reveals host-derived cell-division proteins that are targeted to the cell envelope of a bacterial endosymbiont and involved in its cell division.


Assuntos
Organelas , Simbiose , Bactérias , Eucariotos
5.
PLoS Biol ; 21(1): e3001937, 2023 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-36602948

RESUMO

Apicomplexa are obligate intracellular parasites. While most species are restricted to specific hosts and cell types, Toxoplasma gondii can invade every nucleated cell derived from warm-blooded animals. This broad host range suggests that this parasite can recognize multiple host cell ligands or structures, leading to the activation of a central protein complex, which should be conserved in all apicomplexans. During invasion, the unique secretory organelles (micronemes and rhoptries) are sequentially released and several micronemal proteins have been suggested to be required for host cell recognition and invasion. However, to date, only few micronemal proteins have been demonstrated to be essential for invasion, suggesting functional redundancy that might allow such a broad host range. Cysteine Repeat Modular Proteins (CRMPs) are a family of apicomplexan-specific proteins. In T. gondii, two CRMPs are present in the genome, CRMPA (TGGT1_261080) and CRMPB (TGGT1_292020). Here, we demonstrate that both proteins form a complex that contains the additional proteins MIC15 and the thrombospondin type 1 domain-containing protein (TSP1). Disruption of this complex results in a block of rhoptry secretion and parasites being unable to invade the host cell. In conclusion, this complex is a central invasion complex conserved in all apicomplexans.


Assuntos
Toxoplasma , Animais , Toxoplasma/genética , Toxoplasma/metabolismo , Proteínas de Protozoários/genética , Proteínas de Protozoários/metabolismo , Organelas/metabolismo
6.
Phys Rev Lett ; 130(1): 018401, 2023 Jan 06.
Artigo em Inglês | MEDLINE | ID: mdl-36669211

RESUMO

One of the grand challenges in cellular biophysics is understanding the precision with which cells assemble and maintain subcellular structures. Organelle sizes, for example, must be flexible enough to allow cells to grow or shrink them as environments demand yet be maintained within homeostatic limits. Despite identification of molecular factors that regulate organelle sizes we lack insight into the quantitative principles underlying organelle size control. Here we show experimentally that cells can robustly control average fluctuations in organelle size. By demonstrating that organelle sizes obey a universal scaling relationship we predict theoretically, our framework suggests that organelles grow in random bursts from a limiting pool of building blocks. Burstlike growth provides a general biophysical mechanism by which cells can maintain on average reliable yet plastic organelle sizes.


Assuntos
Organelas , Organelas/fisiologia , Tamanho das Organelas
7.
Nat Commun ; 14(1): 480, 2023 Jan 30.
Artigo em Inglês | MEDLINE | ID: mdl-36717559

RESUMO

Diatoms are unicellular algae characterized by silica cell walls. These silica elements are known to be formed intracellularly in membrane-bound silica deposition vesicles and exocytosed after completion. How diatoms maintain membrane homeostasis during the exocytosis of these large and rigid silica elements remains unknown. Here we study the membrane dynamics during cell wall formation and exocytosis in two model diatom species, using live-cell confocal microscopy, transmission electron microscopy and cryo-electron tomography. Our results show that during its formation, the mineral phase is in tight association with the silica deposition vesicle membranes, which form a precise mold of the delicate geometrical patterns. We find that during exocytosis, the distal silica deposition vesicle membrane and the plasma membrane gradually detach from the mineral and disintegrate in the extracellular space, without any noticeable endocytic retrieval or extracellular repurposing. We demonstrate that within the cell, the proximal silica deposition vesicle membrane becomes the new barrier between the cell and its environment, and assumes the role of a new plasma membrane. These results provide direct structural observations of diatom silica exocytosis, and point to an extraordinary mechanism in which membrane homeostasis is maintained by discarding, rather than recycling, significant membrane patches.


Assuntos
Diatomáceas , Diatomáceas/metabolismo , Parede Celular/metabolismo , Organelas/metabolismo , Dióxido de Silício/química , Exocitose
8.
Cell Mol Life Sci ; 80(2): 53, 2023 Jan 28.
Artigo em Inglês | MEDLINE | ID: mdl-36707427

RESUMO

Chediak-Higashi syndrome (CHS) is a rare, autosomal recessive disorder caused by biallelic mutations in the lysosomal trafficking regulator (LYST) gene. Even though enlarged lysosomes and/or lysosome-related organelles (LROs) are the typical cellular hallmarks of CHS, they have not been investigated in human neuronal models. Moreover, how and why the loss of LYST function causes a lysosome phenotype in cells has not been elucidated. We report that the LYST-deficient human neuronal model exhibits lysosome depletion accompanied by hyperelongated tubules extruding from enlarged autolysosomes. These results have also been recapitulated in neurons differentiated from CHS patients' induced pluripotent stem cells (iPSCs), validating our model system. We propose that LYST ensures the correct fission/scission of the autolysosome tubules during autophagic lysosome reformation (ALR), a crucial process to restore the number of free lysosomes after autophagy. We further demonstrate that LYST is recruited to the lysosome membrane, likely to facilitate the fission of autolysosome tubules. Together, our results highlight the key role of LYST in maintaining lysosomal homeostasis following autophagy and suggest that ALR dysregulation is likely associated with the neurodegenerative CHS phenotype.


Assuntos
Síndrome de Chediak-Higashi , Proteínas de Transporte Vesicular , Humanos , Proteínas de Transporte Vesicular/genética , Lisossomos/fisiologia , Organelas , Autofagia/fisiologia , Síndrome de Chediak-Higashi/genética , Neurônios
9.
Methods Mol Biol ; 2623: 97-111, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-36602682

RESUMO

Long-range transport of organelles and other cellular cargoes along microtubules is driven by kinesin and dynein motor proteins in complex with cargo-specific adaptors. While some adaptors interact exclusively with a single motor, other adaptors interact with both kinesin and dynein motors. However, the mechanisms by which bidirectional motor adaptors coordinate opposing microtubule motors are not fully understood. While single-molecule studies of adaptors using purified proteins can provide key insight into motor adaptor function, these studies may be limited by the absence of cellular factors that regulate or coordinate motor function. As a result, motility assays using cell lysates have been developed to gain insight into motor adaptor function in a more physiological context. These assays are a powerful means to dissect the regulation of motor adaptors as cell lysates contain endogenous microtubule motors and additional factors that regulate motor function. Further, this system is highly tractable as individual proteins can readily be added or removed via overexpression or knockdown in cells. Here, we describe a protocol for in vitro reconstitution of motor-driven transport along dynamic microtubules at single-molecule resolution using total internal reflection fluorescence microscopy of cell lysates.


Assuntos
Dineínas , Proteínas Associadas aos Microtúbulos , Dineínas/metabolismo , Proteínas Associadas aos Microtúbulos/metabolismo , Cinesinas/metabolismo , Microtúbulos/metabolismo , Organelas/metabolismo
10.
Trends Neurosci ; 46(2): 137-152, 2023 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-36635110

RESUMO

Efforts to understand how mitochondrial dysfunction contributes to neurodegeneration have primarily focussed on the role of mitochondria in neuronal energy metabolism. However, progress in understanding the etiological nature of emerging mitochondrial functions has yielded new ideas about the mitochondrial basis of neurological disease. Studies aimed at deciphering how mitochondria signal through interorganellar contacts, vesicular trafficking, and metabolic transmission have revealed that mitochondrial regulation of immunometabolism, cell death, organelle dynamics, and neuroimmune interplay are critical determinants of neural health. Moreover, the homeostatic mechanisms that exist to protect mitochondrial health through turnover via nanoscale proteostasis and lysosomal degradation have become integrated within mitochondrial signalling pathways to support metabolic plasticity and stress responses in the nervous system. This review highlights how these distinct mitochondrial pathways converge to influence neurological health and contribute to disease pathology.


Assuntos
Mitocôndrias , Doenças do Sistema Nervoso , Humanos , Mitocôndrias/metabolismo , Organelas/metabolismo , Homeostase , Transdução de Sinais , Doenças do Sistema Nervoso/metabolismo
11.
Oxid Med Cell Longev ; 2023: 3400147, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-36644574

RESUMO

Apoptosis has been extensively studied, whereas ferroptosis is a newly discovered form of regulated cell death that involves iron-dependent accumulations of lipid hydroperoxides. While these two cell death mechanisms were initially believed to be mutually exclusive, recent studies have revealed cellular contexts requiring a balanced interaction between them. Numerous subcellular sites and signaling molecules within these sites are involved in both processes, either as modules or switches that allow cells to choose on how to proceed. The close relationships between apoptosis and ferroptosis, as well as the possibility of switching from one to the other, are described in this review. To understand the crosstalk between apoptosis and ferroptosis, various organelle-specific mechanisms must be analyzed and compared. The ability to switch apoptosis to ferroptosis by targeting cellular organelles has a great potential in cancer therapy.


Assuntos
Ferroptose , Ferro/metabolismo , Apoptose , Morte Celular , Organelas/metabolismo
12.
Bioinformatics ; 39(1)2023 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-36592044

RESUMO

SUMMARY: Biological condensates are membraneless organelles with different material properties. Proteins and RNAs are the main components, but most of their interactions are still unknown. Here, we introduce PRALINE, a database for the interrogation of proteins and RNAs contained in stress granules, processing bodies and other assemblies including droplets and amyloids. PRALINE provides information about the predicted and experimentally validated protein-protein, protein-RNA and RNA-RNA interactions. For proteins, it reports the liquid-liquid phase separation and liquid-solid phase separation propensities. For RNAs, it provides information on predicted secondary structure content. PRALINE shows detailed information on human single-nucleotide variants, their clinical significance and presence in protein and RNA binding sites, and how they can affect condensates' physical properties. AVAILABILITY AND IMPLEMENTATION: PRALINE is freely accessible on the web at http://praline.tartaglialab.com.


Assuntos
Organelas , RNA , Humanos , RNA/metabolismo , Proteínas/metabolismo , Nucleotídeos/metabolismo
13.
Acc Chem Res ; 56(1): 1-12, 2023 Jan 03.
Artigo em Inglês | MEDLINE | ID: mdl-36533992

RESUMO

ConspectusBiomembranes are ubiquitous lipid structures that delimit the cell surface and organelles and operate as platforms for a multitude of biomolecular processes. The development of chemical tools─fluorescent probes─for the sensing and imaging of biomembranes is a rapidly growing research direction, stimulated by a high demand from cell biologists and biophysicists. This Account focuses on advances in these smart molecules, providing a voyage from the cell frontier─plasma membranes (PM)─toward intracellular membrane compartments─organelles. General classification of the membrane probes can be based on targeting principles, sensing profile, and optical response. Probes for PM and organelle membranes are designed based on multiple targeting principles: conjugation with natural lipids or synthetic targeting ligands and in situ cell labeling by bio-orthogonal chemistry, conjugation to protein tags, and receptor-ligand interactions. Thus, to obtain membrane probes targeting PM with selectivity to one leaflet, we designed membrane anchor ligands based on a charged group and an alkyl chain. According to the sensing profile, we define basic membrane markers with constant emission and probes for biophysical and chemical sensing. The markers are built from classical fluorophores, exemplified by a series of bright cyanines and BODIPY dyes bearing the PM anchors (MemBright). Membrane probes for biophysical sensing are based on environment-sensitive fluorophores: (1) polarity-sensitive solvatochromic dyes; (2) viscosity-sensitive fluorescent molecular rotors; (3) mechanosensitive fluorescent flippers; and (4) voltage-sensitive electrochromic dyes. Our solvatochromic probes based on Nile Red (NR12S, NR12A, NR4A), Laurdan (Pro12A), and 3-hydroxyflavone (F2N12S) through polarity-sensing can visualize liquid ordered and disordered phases of lipid membranes, sense lipid order and its heterogeneity in cell PM, detect apoptosis, etc. Chemically sensitive probes, combining a dye, membrane-targeting ligand, and molecular recognition unit, enable the detection of pH, ions, redox species, lipids, and proteins at the biomembrane surface. In terms of the optical response profile, we can identify (1) fluorogenic (turn-on) probes, allowing background-free imaging; (2) ratiometric probes, e.g., solvatochromic probes, which enable ratiometric imaging by changing their emission/excitation color; (3) fluorescence lifetime-responsive probes, e.g., fluorescence molecular rotors and flippers, suitable for fluorescence lifetime imaging (FLIM); and (4) switchable probes, important for single-molecule localization microscopy. We showed that combining solvatochromic probes with on-off switching through a reversible binding specifically to cell PM enables the mapping of their biophysical properties with superior resolution. While the majority of efforts have been focused on PM, the probes for cellular organelles, such as endoplasmic reticulum, mitochondria, Golgi apparatus, etc., emerge rapidly. Thus, nontargeted solvatochromic probes can distinguish organelles by the emission color. Targeted solvatochromic probes based on Nile Red revealed unique signatures of polarity and lipid order of individual organelles and their different sensitivities to oxidative or mechanical stress. Lipid droplets, which are membraneless lipidic structures, constitute another interesting organelle target for probing the cell stress. Currently, we stand at the beginning of a long route with big challenges ahead, in particular (1) to achieve superior organelle specificity; (2) to label specific biomembrane leaflets, notably the inner leaflet of PM; (3) to detect lipid organization in a proximity of specific proteins; and (4) to probe biomembranes in tissues and animals.


Assuntos
Corantes Fluorescentes , Organelas , Animais , Corantes Fluorescentes/química , Ligantes , Membrana Celular/metabolismo , Lipídeos/química
14.
Virology ; 578: 117-127, 2023 01.
Artigo em Inglês | MEDLINE | ID: mdl-36527930

RESUMO

Picornaviruses rearrange host cell membranes to facilitate their own replication. Here we investigate the Qbc SNARE, SNAP23, which is found at the plasma membrane and plays roles in exocytosis. We found that knockdown of SNAP23 expression inhibits virus replication but not release from cells. Knocking down SNAP23 inhibits viral RNA replication and synthesis of structural proteins. Normal cellular levels of SNAP23 are required for an early step in virus production, prior to or at the stage of virus RNA replication. We report that SNAP23 knockdown generates large, electron-light structures, and that infection of cells with these structures does not alter them, and those cells fail to generate viral RNA replication sites. We suggest that SNAP23 may play a role in maintaining membranes and lipids needed for generating virus replication organelles. Further investigation is needed to determine the precise role of this crucial SNARE protein in EV-D68 replication.


Assuntos
Enterovirus Humano D , Linhagem Celular , Membrana Celular/metabolismo , Enterovirus Humano D/genética , Fusão de Membrana , Organelas , Replicação Viral
15.
Curr Opin Chem Biol ; 72: 102234, 2023 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-36493527

RESUMO

Lipids exert their cellular functions in individual organelles, in some cases on the scale of even smaller, specialized membrane domains. Thus, the experimental capacity to precisely manipulate lipid levels at the subcellular level is crucial for studying lipid-related processes in cell biology. Photo-caged lipid probes which partition into specific cellular membranes prior to photoactivation have emerged as key tools for localized and selective perturbation of lipid concentration in living cells. In this review, we provide an overview of the recent advances in the area and outline which developments are still required for the methodology to be more widely implemented in the wider membrane biology community.


Assuntos
Lipídeos , Organelas , Membrana Celular/metabolismo
16.
J Photochem Photobiol B ; 238: 112624, 2023 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-36521315

RESUMO

Defects in mitochondrial proteostasis contribute to many disorders, including cancer, neurodegeneration, and metabolic and genetic diseases. A strategy aimed at restoring the damaged mitochondrial proteostasis is the mitochondrion-targeting and carrier-free delivery of exogenous functional proteins that can replace the endogenous dysfunctional proteins. The modification of a protein with a photolabile protecting group (PPG, i.e., photocage group) can be activated in situ by response to illumination, leading to release of the protein from its photocage. Here, the Cys and peptide photocages with coumarin were first prepared and characterized for proof of concept. Then, we designed a pair of photocage groups PPG-RhB and PPG-TPP using coumarin and mitochondrion-targeting Rhodamine B (RhB) and triphenylphosphine (TPP), and another pair of organelle-nontarget photocage groups Br-PPG and NO2-PPG for comparison. The proteins modified with these two pairs of photocage groups undergo photolysis in solutions, and can penetrate cell membrane toward their destinations in the carrier-free fashions. The intracellular protein photocages are in situ activated by illumination at 405 nm, and the proteins are released from their photocages in mitochondria and cytoplasm, respectively. This strategy of light-responsive and carrier-free cellular delivery enables mitochondrial and cytoplasmic accumulation of exogenous proteins.


Assuntos
Mitocôndrias , Organelas , Mitocôndrias/metabolismo , Fotólise , Organelas/metabolismo , Peptídeos/metabolismo , Cumarínicos
17.
J Cell Biol ; 222(1)2023 Jan 02.
Artigo em Inglês | MEDLINE | ID: mdl-36542408

RESUMO

Liquid-liquid phase separation (LLPS) has emerged as a fundamental mechanism to compartmentalize biomolecules into membraneless organelles. In this issue, Zhou et al. (2022. J. Cell Biol.https://doi.org/10.1083/jcb.202201088), report that MHV-68 ORF52 undergoes LLPS to form cytoplasmic virion assembly compartments, regulating the spatiotemporal compartmentalization of viral components.


Assuntos
Citoplasma , Herpesviridae , Montagem de Vírus , Citoplasma/virologia , Herpesviridae/fisiologia , Organelas
18.
Int J Biochem Cell Biol ; 154: 106345, 2023 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-36521722

RESUMO

Mitochondria, endoplasmic reticulum and lysosomes are involved in different pathways that can regulate pre-synaptic function. In particular, they could modulate ATP availability in response to rapid changes, could control synaptic protein levels and adjust Ca2+ signalling, which could all impact on neuronal activity. Organelles functions in these processes need to be considered alone when describing the impact of pre-synaptic organelles on neurotransmission. However, the interplay among organelles, which occurs either via signalling pathways or through physical membranous contacts, has to be considered. In this brief review, the physiological role of organelles localized at the pre-synapse in neuronal function is discussed.


Assuntos
Neurônios , Organelas , Organelas/metabolismo , Neurônios/metabolismo , Sinapses/metabolismo , Retículo Endoplasmático/metabolismo , Mitocôndrias/metabolismo , Transmissão Sináptica , Cálcio/metabolismo
19.
Methods Mol Biol ; 2557: 161-209, 2023.
Artigo em Inglês | MEDLINE | ID: mdl-36512216

RESUMO

The Golgi complex (GC) is an essential organelle of the eukaryotic exocytic pathway. It has a very complexed structure and thus localization of its resident proteins is not trivial. Fast development of microscopic methods generates a huge difficulty for Golgi researchers to select the best protocol to use. Modern methods of light microscopy, such as super-resolution light microscopy (SRLM) and electron microscopy (EM), open new possibilities in analysis of various biological structures at organelle, cell, and organ levels. Nowadays, new generation of EM methods became available for the study of the GC; these include three-dimensional EM (3DEM), correlative light-EM (CLEM), immune EM, and new estimators within stereology that allow realization of maximal goal of any morphological study, namely, to achieve a three-dimensional model of the sample with optimal level of resolution and quantitative determination of its chemical composition. Methods of 3DEM have partially overlapping capabilities. This requires a careful comparison of these methods, identification of their strengths and weaknesses, and formulation of recommendations for their application to cell or tissue samples. Here, we present an overview of 3DEM methods for the study of the GC and some basics for how the images are formed and how the image quality can be improved.


Assuntos
Elétrons , Complexo de Golgi , Microscopia Eletrônica , Complexo de Golgi/ultraestrutura , Organelas , Algoritmos
20.
Biomacromolecules ; 24(1): 283-293, 2023 Jan 09.
Artigo em Inglês | MEDLINE | ID: mdl-36511362

RESUMO

The membrane-less organelles (MLOs) with subcompartments are formed via liquid-liquid phase separation (LLPS) in the crowded cell interior whose background molecules are up to 400 mg/mL. It is still a puzzle how the background molecules regulate the formation, dynamics, and functions of MLOs. Using biphasic coacervate droplets formed by poly(l-lysine) (PLL), quaternized dextran (Q-dextran), and single-stranded oligonucleotides (ss-oligo) as a model of MLO, we online monitored the LLPS process in Bovine Serine Albumin (BSA) solution up to 200.0 mg/mL. Negatively charged BSA is able to form complex or coacervate with positively charged PLL and Q-dextran and thus participates in the LLPS via nonspecific interactions. Results show that BSA effectively regulates the LLPS by controlling the phase distribution, morphologies, and kinetics. With increasing BSA concentration, the spherical biphasic droplets evolve in sequence into phase-inverted flower-like structure, worm-like chains, network structures, and confined coacervates. Each kind of morphology is formed via its own specific growth and fusion pathway. Our work suggests that MLOs could be controlled solely by the crowded environment and provides a further step toward understanding the life process in cell.


Assuntos
Biopolímeros , Dextranos , Lisina , Organelas , Soroalbumina Bovina/química , Biopolímeros/química
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...