Abstract. A high-performance, all-sky imaging system has been used to obtain novel data on the morphology and dynamics of short-period (<1 hour) gravity waves at equatorial latitudes. Gravity waves imaged in the upper mesosphere and lower thermosphere were recorded in three nightglow emissions, the near-infrared OH emission, and the visible wavelength OI (557.7 nm) and Na (589.2 nm) emissions spanning the altitude range ---80-100 km. The measurements were made from Alcantara, Brazil (2.3øS, 44.5øW), during the period August-October 1994 as part of the NASA/Instituto Nacional de Pesquisas Espaciais "Guara campaign". Over 50 wave events were imaged from which a statistical study of the characteristics of equatorial gravity waves has been performed. The data were found to divide naturally into two groups. The first group corresponded to extensive, freely propagating (or ducted) gravity waves with observed periods ranging from 3.7 to
Actin is one of the most ubiquitous, abundant and well-conserved proteins of eukaryotes, participating in many crucial cellular processes including the maintenance of cell shape, motility and cell division. Actins from the most divergent sources still share amino-acid identities in excess of 70% (ref. 3). This may well explain why low-abundance homologues of actin have been difficult to isolate. Genes encoding distant relatives of actin in budding and fisson yeast have now been cloned. We report here the discovery of a vertebrate actin-like protein, which we name centractin. A full-length complementary DNA clone was isolated whose sequence reveals amino-acid identities with actin of over 50%, increasing to more than 70% when conservative amino-acid changes are considered. Northern analysis and western blotting indicate a ubiquitous tissue and species distribution. Morphological and biochemical criteria show that centractin is associated with centrosomes.
Mutation of the lysosomal hydrolase acid-β-glucosidase (GCase), which leads to reduced GCase activity, is one of the most frequent genetic risk factors for Parkinson's disease (PD) and promotes α-synuclein accumulation in the brain, a hallmark of PD and other synucleinopathies. Whether targeting GCase pharmacologically is a valid therapeutic strategy for sporadic PD in the absence of GCase mutation is unknown. We have investigated whether increasing the stability, trafficking, and activity of wild-type GCase could be beneficial in synucleinopathies by administering the pharmacological chaperone AT2101 (afegostat-tartrate, isofagomine) to mice that overexpress human wild-type α-synuclein (Thy1-aSyn mice). AT2101 administered orally for 4 months to Thy1-aSyn mice improved motor and nonmotor function, abolished microglial inflammatory response in the substantia nigra, reduced α-synuclein immunoreactivity in nigral dopaminergic neurons, and reduced the number of small α-synuclein aggregates, while increasing the number of large α-synuclein aggregates. These data support the further investigation of pharmacological chaperones that target GCase as a therapeutic approach for sporadic PD and other synucleinopathies, even in the absence of glucocerebrosidase mutations.
As part of our ongoing efforts to understand the functional role of vertebrate centractins, we have identified a new member of the actin- related family of proteins in the yeast Saccharomyces cerevisiae using a PCR-based approach. Consistent with the current nomenclature for actin-related proteins in yeast, we propose to denote this locus ACT3. The primary amino acid sequence of Act3p is most similar to canine and human alpha-centractin (73% similarity/54% identity). The sequence of a genomic clone indicates ACT3 lies adjacent to and is transcribed convergently with respect to FUR1 on chromosome VIII. Molecular genetic analysis indicates ACT3 is represented by a single gene from which the corresponding mRNA is expressed at a low level compared to ACT1. Tetrad analysis of heterozygotes harboring a TRP1 replacement of the ACT3- coding region indicates ACT3 is nonessential for growth under normal conditions and at extremes of temperature and osmolarity. However, growth at 14 degrees C indicates a spindle orientation defect similar to phenotypes recently described for yeast harboring mutations in actin, tubulin, or cytoplasmic dynein. Taken together, our data suggest that ACT3 is the S. cerevisiae homologue of vertebrate centractins.
Observations and theory of convectively coupled equatorial waves suggest that they can be categorized into two distinct groups. Moisture modes are waves whose thermodynamics are governed by moisture fluctuations. The thermodynamics of the gravity wave group, on the other hand, are rooted in buoyancy (temperature) fluctuations. On the basis of scale analysis, it is found that a simple nondimensional parameter—akin to the Rossby number—can explain the processes that lead to the existence of these two groups. This parameter, defined as Nmode, indicates that moisture modes arise when anomalous convection lasts sufficiently long so that dry gravity waves eliminate the temperature anomalies in the convective region, satisfying weak temperature gradient (WTG) balance. This process causes moisture anomalies to dominate the distribution of moist enthalpy (or moist static energy), and hence the evolution of the wave. Conversely, convectively coupled gravity waves arise when anomalous convection eliminates the moisture anomalies more rapidly than dry gravity waves can adjust the troposphere toward WTG balance, causing temperature to govern the moist enthalpy distribution and evolution. Spectral analysis of reanalysis data indicates that slowly propagating waves (cp ~ 3 m s−1) are likely to be moisture modes while fast waves (cp ~ 30 m s−1) exhibit gravity wave behavior, with “mixed moisture–gravity” waves existing in between. While these findings are obtained from a highly idealized framework, it is hypothesized that they can be extended to understand simulations of convectively coupled waves in GCMs and the thermodynamics of more complex phenomena.
The covalent oligomer formation is blocked in the presence of a sulfhydryl-modifying reagent. We propose that there are two stages in this Vp1 disulfide bonding. First, the newly synthesized Vp1 monomers acquire intrachain bonds as they fold and begin to interact. Next, these bonds are replaced with intermolecular bonds as the monomers assemble into pentamers. This sequential appearance of transitory disulfide bonds is consistent with a role for sulfhydryldisulfide redox reactions in the coordinate folding of Vp1 chains into pentamers. The cytoplasmic Vp1 does not colocalize with marker proteins of the endoplasmic reticulum. This paper demonstrates in vivo disulfide formations and exchanges coupled to the folding and oligomerization of a mammalian protein in the cytoplasm, outside the secretory pathway. Such disulfide dynamics may be a general phenomenon for other cysteine-bearing mammalian proteins that fold in the cytoplasm. H ow proteins fold into functional, three-dimensional structures has been under intense study (1), and the folding pathways for a number of eukaryotic proteins have been characterized in vitro (2, 3) or in vivo (4-9). In the secretory pathway, protein folding is coupled to the formation and reshuffling of disulfide bonds. These redox conversions, leading to native, disulfide-bonded proteins, are catalyzed by prokaryotic Dsb proteins in the periplasm (10-12) and eukaryotic protein disulfide isomerase (PDI) in the endoplasmic reticulum (ER) (13-16). Proteins that fold and assemble in the reducing environment of the cytoplasm generally do not harbor native disulfides, owing to the activities of thioredoxins and glutaredoxins. Transitory disulfide bonding, though, is required for the folding of bacteriophage P22 tailspike protein in the cytoplasm (17, 18). Whether disulfide bond-coupled folding pathways exist for nonsecretory proteins in the mammalian cytoplasm is not known.The structure of simian virus 40 (SV40), known at the atomic resolution, is determined by the major capsid protein Vp1 (19). Seventy-two pentamers of Vp1 form the outer shell of SV40, with each monomer making contact with its four intrapentamer neighbors via interdigitating secondary structural elements. The Vp1 pentamer is expected to form in the cytoplasm of SV40-infected cells during or soon after the monomers' synthesis (20, 21). There are seven cysteine residues in one Vp1 chain. No intrapentamer disulfide bridges, either between or within the monomers, are observed in the mature particle (22). Certain cysteine residues do lie in close proximity of one another, such as the Cys-49-Cys-87 and Cys-87-Cys-207 pairs within one monomer and the Cys-49-Cys-207 pair between two monomers within a pentamer (19). Each cysteine pair conceivably can become juxtaposed during the folding process and form a transient disulfide bond.In this study, we show that in the virus-infected cytoplasm, the newly synthesized Vp1 chain is an intramolecularly disulfidebonded monomer and is a precursor for intermolecularly disulfidebonded Vp1 oligome...
In this study we implement eight lightning parameterizations in the Community Atmospheric Model (CAM5), evaluate the performance of the parameterizations in the present climate, and test the sensitivity of future lightning activity to the choice of parameterization. In the present day, the annual mean lightning flash densities in simulations constrained by reanalysis data show the highest spatial correlation to satellite observations for parameterizations based either on cloud top height (0.83) or cold cloud depth (0.80). Under future scenarios using representative concentration pathways, changes in global mean lightning flash density are highly sensitive to the parameterization chosen, with cloud top height schemes, a cold cloud depth scheme, and a scheme based on convective mass flux projecting large increases (36% to 45%), a mild increase (12.6%), and a decrease (−6.7%) in lightning flash density, respectively, under the RCP8.5 scenario, which causes a 3.4 K warming between 1996–2005 and 2079–2088.
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