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Disordered proteins have long been known to help mediate tolerance to different abiotic stresses including freezing, osmotic stress, high temperatures, and desiccation in a diverse set of organisms. Recently, three novel families of intrinsically disordered proteins were identified in tardigrades, microscopic animals capable of surviving a battery of environmental extremes. These three families include the Cytoplasmic-, Secreted-, and Mitochondrial- Abundant Heat Soluble (CAHS, SAHS, and MAHS) proteins, which are collectively termed Tardigrade Disordered Proteins (TDPs). At the level of sequence conservation TDPs are unique to tardigrades, and beyond their high degree of disorder the CAHS, SAHS, and MAHS families do not resemble one another. All three families are either highly expressed constitutively, or significantly enriched in response to desiccation. In vivo, ex vivo, and in vitro experiments indicate functional roles for members of each TDP family in mitigating cellular perturbations induced by various abiotic stresses. What is currently lacking is a comprehensive and holistic understanding of the fundamental mechanisms by which TDPs function, and the properties of TDPs that allow them to function via those mechanisms. A quantitative and systematic approach is needed to identify precisely what cellular damage TDPs work to prevent, what sequence features are important for these functions, and how those sequence features contribute to the underlying mechanisms of protection. Such an approach will inform us not only about these fascinating proteins, but will also provide insights into how the sequence of a disordered protein can dictate its functional, structural, and dynamic properties. B9H8mivzozNw77APwM7Egm Video Abstract Graphical abstract

The plants are exposed to different abiotic stresses, including the salinity stress (SS) that negatively affect the growth, metabolism, physiological and biochemical processes. Thus, this study investigated the effect of diverse levels of foliar-applied GB (0 control, 50 mM and 100 mM) on maize growth, membrane stability, physiological and biochemical attributes, antioxidant enzymes and nutrients accumulation under different levels of SS (i.e., control, 6 dS m-1, 12 dS m-1). Salt stress diminished the root and shoot length, root and shoot biomass, chlorophyll contents, photosynthetic rate (Pn), stomatal conductance (gs), relative water contents (RWC), soluble proteins (SP) and free amino acids; (FAA); and increased activities of antioxidant enzymes, electrical conductivity (EC) and accumulation of malondialdehyde (MDA), hydrogen peroxide (H2O2), Na+ and Cl− ions. GB application significantly increased root and shoot growth, leaves per plant, shoots length, chlorophyll contents, gs, Pn and membrane stability by reducing MDA and H2O2 accumulation. Moreover, GB also increased the SP, FAA accumulation, activities of antioxidant enzymes and Na+ and Cl- exclusion by favouring Ca2+ and K+ accumulation. In conclusion, the foliar-applied GB increased Pn, gs, ant-oxidants activities, and accumulation of SP and FAA; and reduced the accretion of Na+ and Cl− by favouring the Ca2+ and K+ accretion which in turns improved growth under SS.

The total soluble protein-mediated morphological traits in mustard treated with Thiourea and Salicylic acid were investigated. In addition, it tested the hypothesis that the growth regulator salicylic acid protects the photosynthetic apparatus by up-regulating morphological traits. Under natural environmental conditions, seeds were sown in the field, and seed emergence was recorded. For three days after the 15-day stage, plants in the area were treated with thiourea and salicylic acid and allowed to grow for 90 days. Plants were harvested to assess various morphological traits. A follow-up application of SA and Thiourea plants improved plant height, leaf area, internodal length, leaf number, and accelerated plant activity. The up-regulation of morphological traits may have occurred in SA and Thiourea-mediated plants. After treatments, the level of total soluble protein was estimated in the leaves at proposed day intervals.

Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone which is essential in eukaryotes. It is required for the activation and stabilization of a wide variety of client proteins and many of them are involved in important cellular pathways. Since Hsp90 affects numerous physiological processes such as signal transduction, intracellular transport, and protein degradation, it became an interesting target for cancer therapy. Structurally, Hsp90 is a flexible dimeric protein composed of three different domains which adopt structurally distinct conformations. ATP binding triggers directionality in these conformational changes and leads to a more compact state. To achieve its function, Hsp90 works together with a large group of cofactors, termed co-chaperones. Co-chaperones form defined binary or ternary complexes with Hsp90, which facilitate the maturation of client proteins. In addition, posttranslational modifications of Hsp90, such as phosphorylation and acetylation, provide another level of regulation. They influence the conformational cycle, co-chaperone interaction, and inter-domain communications. In this review, we discuss the recent progress made in understanding the Hsp90 machinery.

Background： Brain acid soluble protein 1 （BASPI） is identified as a novel potential tumor suppressor in several cancers. However, its role in thyroid cancer has not been investigated yet. In the present study, the antitumor activities of BASP1 against the growth and migration of thyroid cancer cells were evaluated. Methods： BASP1 expression in thyroid cancer tissues and normal tissues were examined by immunohistochemical staining and the association between its expression and prognosis was analyzed, pcDNA-BASP 1 carrying full length of BASP1 cDNA was constructed to restore the expression of BASP1 in thyroid cancer cell lines （BHT- I 01 and KMH-2）. The cell proliferation in vitro and in vivo was evaluated by WST-1 assay and xenografl tumor models, respectively. Cell cycle distribution after transfection was analyzed using flow cytometry. Cell apoptosis after transfection was examined by annexin V/propidium iodide assay. The migration was examined using transwell assay. Results： BASP1 expression was abundant in normal tissues while it is significantly decreased in cancer tissues （P = 0.000）. pcDNA-BASP1 restored the expression of BASPI and significantly inhibited the growth of BHT-101 and KMH-2 cells as well as xenograft tumors in nude mice （P = 0.000）. pcDNA-BASPI induced G1 arrest and apoptosis in BHT-101 and KMH-2 cells. In addition, pcDNA-BASP1 significantly inhibited the cell migration. Conclusions： Downregulation of BASP1 expression may play a role in the tumorigenesis of thyroid cancer. Restoration of BASPI expression exerted extensive antitumor activities against growth and migration of thyroid cancer cells, which suggested that BASPI gene might act as a potential therapeutic agent for the treatment of thyroid cancer.

The mechanism of transport through the Golgi complex is not completely understood, insofar as no single transport mechanism appears to account for all of the observations. Here, we compare the transport of soluble secretory proteins (albumin and α1-antitrypsin) with that of supramolecular cargoes (e.g., procollagen) that are proposed to traverse the Golgi by compartment progression–maturation. We show that these soluble proteins traverse the Golgi much faster than procollagen while moving through the same stack. Moreover, we present kinetic and morphological observations that indicate that albumin transport occurs by diffusion via intercisternal continuities. These data provide evidence for a transport mechanism that applies to a major class of secretory proteins and indicate the co-existence of multiple intra-Golgi trafficking modes. The Golgi is a structure within cells where proteins and other large molecules are modified and prepared for delivery to locations inside or outside of the cell. Each Golgi is made from a stack of flattened sacs called cisternae that are filled with fluid and enclosed by a membrane. Proteins and other molecules are transported to the Golgi by packages called vesicles, which fuse with the outermost cisterna, which is known as the ‘cis-face’ of the Golgi, and unload their contents. From here, the proteins are processed and modified by enzymes as they move through the Golgi towards the ‘trans-face’ on the opposite side. The modified proteins are then re-packaged into vesicles before being sent to their intended destinations. But how do proteins move through the Golgi? Some researchers have suggested that proteins do not actually move: rather, the stacks of the Golgi move like a conveyer belt as new cisterna are added to the cis-face. However, other researchers have proposed that molecules proceed from one cisterna to the next inside small vesicles. It is also possible that proteins are transported through the Golgi in other ways, or by a combination of two or more methods. Now, Beznoussenko, Parashuraman et al. reveal that some small, soluble, proteins can move through the Golgi by diffusion. These proteins move much quicker than large protein complexes, which suggests that multiple transport mechanisms do co-exist within the Golgi. Furthermore, Beznoussenko, Parashuraman et al. found that these soluble proteins are most likely moving through some narrow tunnel-like connections between the individual cisternae. Following on from the work of Beznoussenko, Parashuraman et al., the main challenge is to understand how all the different types of proteins that move through the Golgi are transported—which includes roughly a third of all human proteins. As many of these proteins are important for human health, learning to control their transport might create new opportunities to understand and treat disease.

Abstract Myxobolus koi is one species of Myxobolus sp that can cause parasitic diseases in fish called Myxobolusis. Based on the Decree of the Minister of Marine and Fisheries No: KEP.03/MEN/2010 that Myxobolus koi in the list of Fish Quarantine Pests group I. Myxosporean diseases are most numerous in the water can cause Proliferative Kidney Disease (PKD) and Whirling Disease (WD). The aim of this research is to finding, analyzing and determining the protein of spores Myxobolus koi that can effectively reduce the level of damage to the intestinal organs as well as for the prevention myxobolusis on Koi’s. Then for finding, analyzing and determining the protein of spores Myxobolus koi do isolation of spore proteins. The study consisted of three phases examination to preparation and identification of spores, isolation and analyze of crude and soluble protein spores for obtain dose and molecular weight each protein and histopathological test. This research uses descriptive method. The data presented may be narratives, images, tables or charts for each group. Intestinal histopathology test results of research carried scoring Koi’s were analyzed using the Kruskal-Wallis. The results showed a profile crude protein and soluble proteins from spores Myxobolus koi showed that the molecular weight of crude protein Myxobolus koi in this study was 150 kDa and 72 kDa and for soluble protein was 73 kDa. Results scoring the degree of infection caused by exposure to Myxobolus koi then statistically processed with an average yield of scoring in a sequence of 0; 1.6; 0.64 and 0.32. Statistical analysis showed no significant difference in the treatment of K + with crude protein, and K + with soluble proteins. Statistical analysis showed that there were significant differences in treatment with K+ and K-, K- with soluble protein and crude protein and soluble protein. Histopathological changes in the intestine in the form of inflammatory cell infiltration, necrosis and haemorage

Evolutionarily conserved SNARE (soluble N -ethylmaleimide sensitive factor attachment protein receptors) proteins form a complex that drives membrane fusion in eukaryotes. The ATPase NSF ( N -ethylmaleimide sensitive factor), together with SNAPs (soluble NSF attachment protein), disassembles the SNARE complex into its protein components, making individual SNAREs available for subsequent rounds of fusion. Here we report structures of ATP- and ADP-bound NSF, and the NSF/SNAP/SNARE (20S) supercomplex determined by single-particle electron cryomicroscopy at near-atomic to sub-nanometre resolution without imposing symmetry. Large, potentially force-generating, conformational differences exist between ATP- and ADP-bound NSF. The 20S supercomplex exhibits broken symmetry, transitioning from six-fold symmetry of the NSF ATPase domains to pseudo four-fold symmetry of the SNARE complex. SNAPs interact with the SNARE complex with an opposite structural twist, suggesting an unwinding mechanism. The interfaces between NSF, SNAPs, and SNAREs exhibit characteristic electrostatic patterns, suggesting how one NSF/SNAP species can act on many different SNARE complexes. Using single-particle electron cryomicroscopy, several structures are reported which illuminate the mechanisms of action of the ATPase NSF that disassembles the SNARE complex into individual protein components. SNARE protein recycling mechanism In a variety of cellular processes — including neurotransmitter release, hormone release and vesicle trafficking — the evolutionarily conserved SNARE proteins form a complex that drives fusion between membranes of two cellular compartments. Once fusion occurs, these complexes are disassembled by the ATPase enzyme NSF and the SNAP adaptor proteins to recycle individual SNAREs for another round of membrane fusion. This study reports the use of single-particle electron cryomicroscopy to determine sub-nanometre to near-atomic resolution structures of NSF and the 20S complex. This paper reports the structures of full-length NSF in ATP- and ADP-bound states, and those of the roughly 660-kilodalton NSF/SNAP/SNARE (20S) super-complex involving two different SNARE complexes. The authors' data provide unprecedented details of the inner-workings of these essential molecular machines.

Predicting protein-ligand binding free energy rapidly and accurately remains a challenging question in modern drug discovery. Molecular mechanics/Poisson-Boltzmann (Generalized Born) surface area (MM/PB(GB)SA) has emerged as an essential tool for accelerating cost-efficient binding free energy calculation. This study presents benchmarks with three membrane-bound protein systems and six soluble protein systems. Different parameters were sampled for different benchmarks to explore the highest accuracy. These include ligand charges, protein force fields, extra points, GB models, nonpolar optimization methods, internal dielectric constants and membrane dielectric constants. Comparisons of accuracy were made between MM/PB(GB)SA, docking and free energy perturbation (FEP). The results reveal a competitive performance between MM/PB(GB)SA and FEP. In summary, MM/PB(GB)SA is a powerful approach to predict ligand binding free energy rapidly and accurately. Parameters of MM/PB(GB)SA calculations, such as the GB models and membrane dielectric constants, need to be optimized for different systems. This method can be served as a powerful tool for drug design.

NAC transcription factors are commonly involved in the plant response to drought stress. A transcriptome analysis of root samples of the soybean variety ‘Jiyu47’ under drought stress revealed the evidently up-regulated expression of GmNAC19, consistent with the expression pattern revealed by quantitative real-time PCR analysis. The overexpression of GmNAC19 enhanced drought tolerance in Saccharomyces cerevisiae INVSc1. The seed germination percentage and root growth of transgenic Arabidopsis thaliana were improved in comparison with those of the wild type, while the transgenic soybean composite line showed improved chlorophyll content. The altered contents of physiological and biochemical indices (i.e., soluble protein, soluble sugar, proline, and malondialdehyde) related to drought stress and the activities of three antioxidant enzymes (i.e., superoxide dismutase, peroxidase, and catalase) revealed enhanced drought tolerance in both transgenic Arabidopsis and soybean. The expressions of three genes (i.e., P5CS, OAT, and P5CR) involved in proline synthesis were decreased in the transgenic soybean hairy roots, while the expression of ProDH involved in the breakdown of proline was increased. This study revealed the molecular mechanisms underlying drought tolerance enhanced by GmNAC19 via regulation of the contents of soluble protein and soluble sugar and the activities of antioxidant enzymes, providing a candidate gene for the molecular breeding of drought-tolerant crop plants.