Nonextensivity of the cyclic Lattice Lotka Volterra model

We numerically show that the Lattice Lotka-Volterra model, when realized on a square lattice support, gives rise to a {\it finite} production, per unit time, of the nonextensive entropy $S_q= \frac{1- \sum_ip_i^q}{q-1}$ $(S_1=-\sum_i p_i \ln p_i)$. This finiteness only occurs for $q=0.5$ for the $d=2$ growth mode (growing droplet), and for $q=0$ for the $d=1$ one (growing stripe). This strong evidence of nonextensivity is consistent with the spontaneous emergence of local domains of identical particles with fractal boundaries and competing interactions. Such direct evidence is for the first time exhibited for a many-body system which, at the mean field level, is conservative.Comment: Latex, 6 pages, 5 figure

Magneto-transport and magnetic susceptibility of SmFeAsO1-xFx (x = 0.0 and 0.20)

Bulk polycrystalline samples, SmFeAsO and the iso-structural superconducting SmFeAsO0.80F0.20 are explored through resistivity with temperature under magnetic field {\rho}(T, H), AC and DC magnetization (M-T), and Specific heat (Cp) measurements. The Resistivity measurement shows superconductivity for x = 0.20 sample with Tc(onset) ~ 51.7K. The upper critical field, [Hc2(0)] is estimated ~3770kOe by Ginzburg-Landau (GL) theory. Broadening of superconducting transition in magneto transport is studied through thermally activated flux flow in applied field up to 130 kOe. The flux flow activation energy (U/kB) is estimated ~1215K for 1kOe field. Magnetic measurements exhibited bulk superconductivity with lower critical field (Hc1) of ~1.2kOe at 2K. In normal state, the paramagnetic nature of compound confirms no trace of magnetic impurity which orders ferromagnetically. AC susceptibility measurements have been carried out for SmFeAsO0.80F0.20 sample at various amplitude and frequencies of applied AC drive field. The inter-granular critical current density (Jc) is estimated. Specific heat [Cp(T)] measurement showed an anomaly at around 140K due to the SDW ordering of Fe, followed by another peak at 5K corresponding to the antiferromagnetic (AFM) ordering of Sm+3 ions in SmFeAsO compound. Interestingly the change in entropy (marked by the Cp transition height) at 5K for Sm+3 AFM ordering is heavily reduced in case of superconducting SmFeAsO0.80F0.20 sample.Comment: 18 pages text + Figs: comments/suggestions welcome ([email protected]

Anomalous diffusion with absorption: Exact time-dependent solutions

Recently, analytical solutions of a nonlinear Fokker-Planck equation describing anomalous diffusion with an external linear force were found using a non extensive thermostatistical Ansatz. We have extended these solutions to the case when an homogeneous absorption process is also present. Some peculiar aspects of the interrelation between the deterministic force, the nonlinear diffusion and the absorption process are discussed.Comment: RevTex, 16 pgs, 4 figures. Accepted in Physical Review

Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pump

The MtrCDE multidrug pump, from Neisseria gonorrhoeae, is assembled from the inner and outer membrane proteins MtrD and MtrE, which are connected by the periplasmic membrane fusion protein MtrC. Although it is clear that MtrD delivers drugs to the channel of MtrE, it remains unclear how drug delivery and channel opening are connected. We used a vancomycin sensitivity assay to test for opening of the MtrE channel. Cells expressing MtrE or MtrE-E434K were insensitive to vancomycin; but became moderately and highly sensitive to vancomycin respectively, when coexpressed with MtrC, suggesting that the MtrE channel opening requires MtrC binding and is energy-independent. Cells expressing wild-type MtrD, in an MtrCE background, were vancomycin-insensitive, but moderately sensitive in an MtrCE-E434K background. The mutation of residues involved in proton translocation inactivated MtrD and abolished drug efflux, rendered both MtrE and MtrE-E434K vancomycin-insensitive; imply that the pump–component interactions are preserved, and that the complex is stable in the absence of proton flux, thus sealing the open end of MtrE. Following the energy-dependent dissociation of the tripartite complex, the MtrE channel is able to reseal, while MtrE-E434K is unable to do so, resulting in the vancomycin-sensitive phenotype. Thus, our findings suggest that opening of the OMP via interaction with the MFP is energy-independent, while both drug export and complex dissociation require active proton flux

Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pump

The MtrCDE multidrug pump, from Neisseria gonorrhoeae, is assembled from the inner and outer membrane proteins MtrD and MtrE, which are connected by the periplasmic membrane fusion protein MtrC. Although it is clear that MtrD delivers drugs to the channel of MtrE, it remains unclear how drug delivery and channel opening are connected. We used a vancomycin sensitivity assay to test for opening of the MtrE channel. Cells expressing MtrE or MtrE-E434K were insensitive to vancomycin; but became moderately and highly sensitive to vancomycin respectively, when coexpressed with MtrC, suggesting that the MtrE channel opening requires MtrC binding and is energy-independent. Cells expressing wild-type MtrD, in an MtrCE background, were vancomycin-insensitive, but moderately sensitive in an MtrCE-E434K background. The mutation of residues involved in proton translocation inactivated MtrD and abolished drug efflux, rendered both MtrE and MtrE-E434K vancomycin-insensitive; imply that the pump-component interactions are preserved, and that the complex is stable in the absence of proton flux, thus sealing the open end of MtrE. Following the energy-dependent dissociation of the tripartite complex, the MtrE channel is able to reseal, while MtrE-E434K is unable to do so, resulting in the vancomycin-sensitive phenotype. Thus, our findings suggest that opening of the OMP via interaction with the MFP is energy-independent, while both drug export and complex dissociation require active proton flux

A Gβ protein and the TupA co-regulator bind to protein kinase a Tpk2 to act as antagonistic molecular switches of fungal morphological changes

The human pathogenic fungus Paracoccidioides brasiliensis (Pb) undergoes a morphological transition from a saprobic mycelium to pathogenic yeast that is controlled by the cAMP-signaling pathway. There is a change in the expression of the Gβ-protein PbGpb1, which interacts with adenylate cyclase, during this morphological transition. We exploited the fact that the cAMP-signaling pathway of Saccharomyces cerevisiae does not include a Gβ-protein to probe the functional role of PbGpb1. We present data that indicates that PbGpb1 and the transcriptional regulator PbTupA both bind to the PKA protein PbTpk2. PbTPK2 was able to complement a TPK2Δ strain of S. cerevisiae, XPY5a/α, which was defective in pseudohyphal growth. Whilst PbGPB1 had no effect on the parent S. cerevisiae strain, MLY61a/α, it repressed the filamentous growth of XPY5a/α transformed with PbTPK2, behaviour that correlated with a reduced expression of the floculin FLO11. In vitro, PbGpb1 reduced the kinase activity of PbTpk2, suggesting that inhibition of PbTpk2 by PbGpb1 reduces the level of expression of Flo11, antagonizing the filamentous growth of the cells. In contrast, expressing the co-regulator PbTUPA in XPY5a/α cells transformed with PbTPK2, but not untransformed cells, induced hyperfilamentous growth, which could be antagonized by co-transforming the cells with PbGPB1. PbTUPA was unable to induce the hyperfilamentous growth of a FLO8Δ strain, suggesting that PbTupA functions in conjunction with the transcription factor Flo8 to control Flo11 expression. Our data indicates that P. brasiliensis PbGpb1 and PbTupA, both of which have WD/β-propeller structures, bind to PbTpk2 to act as antagonistic molecular switches of cell morphology, with PbTupA and PbGpb1 inducing and repressing filamentous growth, respectively. Our findings define a potential mechanism for controlling the morphological switch that underpins the virulence of dimorphic fungi

Scarabaeoidea (Insecta : Coleoptera) in the Brazilian Cerrado : current state of knowledge

Besouros pertencentes à superfamília Scarabaeoidea ocupam habitats variados, possuem hábitos alimentares diversifi cados, desempenham importante papel ecológico e diversas espécies apresentam importância agrícola. No entanto, estudos com esse grupo na região do Cerrado são escassos. Nesta revisão realizou-se um levantamento dos artigos publicados nos últimos 30 anos a respeito dos Scarabaeoidea no Cerrado. Foram recuperados 64 artigos, realizados em nove unidades da federação, que focavam quatro temas principais espécies praga, aspectos bioecológicos, biodiversidade e importância ecológica, e técnicas e metodologias de coleta de Scarabaeoidea. Os resultados desta revisão indicam que poucos estudos foram realizados com os Scarabaeoidea no Cerrado brasileiro nas últimas décadas frente à importância e diversidade desse grupo de insetos.Beetles belonging to the superfamily Scarabaeoidea occupy different habitats, present feeding habits diversifi ed, play an important ecological role and several species have agricultural importance. However, studies with this group in the Brazilian Cerrado are scarce. In this review we carried out a survey of scientifi c articles published in the past 30 years concerning Scarabaeoidea in the Cerrado. Were found 64 studies in nine Brazilian states. The studies focused on four main topics: pest species, bioecology, biodiversity and ecological importance, techniques and methodologies for collecting Scarabaeoidea. The results of this review indicate that few studies have been conducted with Scarabaeoidea in the Cerrado in recent decades compared to the importance and diversity of this group of insects

Opening of the outer membrane protein channel in tripartite efflux pumps is induced by interaction with the membrane fusion partner

The multiple transferable resistance (MTR) pump, from Neisseria gonorrhoeae, is typical of the specialized machinery used to translocate drugs across the inner and outer membranes of Gram-negative bacteria. It consists of a tripartite complex composed of an inner-membrane transporter, MtrD, a periplasmic membrane fusion protein, MtrC, and an outer-membrane channel, MtrE. We have expressed the components of the pump in Escherichia coli and used the antibiotic vancomycin, which is too large to cross the outer-membrane by passive diffusion, to test for opening of the MtrE channel. Cells expressing MtrCDE are not susceptible to vancomycin, indicating that the channel is closed; but become susceptible to vancomycin in the presence of transported substrates, consistent with drug-induced opening of the MtrE channel. A mutational analysis identified residues Asn-198, Glu-434, and Gln-441, lining an intraprotomer groove on the surface of MtrE, to be important for pump function; mutation of these residues yielded cells that were sensitive to vancomycin. Pull-down assays and micro-calorimetry measurements indicated that this functional impairment is not due to the inability of MtrC to interact with the MtrE mutants; nor was it due to the MtrE mutants adopting an open conformation, because cells expressing these MtrE mutants alone are relatively insensitive to vancomycin. However, cells expressing the MtrE mutants with MtrC are sensitive to vancomycin, indicating that residues lining the intra-protomer groove control opening of the MtrE channel in response to binding of MtrC

Evidence for the assembly of a bacterial tripartite multidrug pump with a stoichiometry of 3: 6: 3

The multiple transferable resistance (mTR) pump from Neisseria gonorrhoeae MtrCDE multidrug pump is assembled from the inner and outer membrane proteins MtrD and MtrE and the periplasmic membrane fusion protein MtrC. Previously we established that while there is a weak interaction of MtrD and MtrE, MtrC binds with relatively high affinity to both MtrD and MtrE. MtrD conferred antibiotic resistance only when it was expressed with MtrE and MtrC, suggesting that these proteins form a functional tripartite complex in which MtrC bridges MtrD and MtrE. Furthermore, we demonstrated that MtrC interacts with an intraprotomer groove on the surface of MtrE, inducing channel opening. However, a second groove is apparent at the interface of the MtrE subunits, which might also be capable of engaging MtrC. We have now established that MtrC can be cross-linked to cysteines placed in this interprotomer groove and that mutation of residues in the groove impair the ability of the pump to confer antibiotic resistance by locking MtrE in the closed channel conformation. Moreover, MtrE K390C forms an intermolecular disulfide bond with MtrC E149C locking MtrE in the open channel conformation, suggesting that a functional salt bridge forms between these residues during the transition from closed to open channel conformations. MtrC forms dimers that assemble into hexamers, and electron microscopy studies of single particles revealed that these hexamers are arranged into ring-like structures with an internal aperture sufficiently large to accommodate the MtrE trimer. Cross-linking of single cysteine mutants of MtrC to stabilize the dimer interface in the presence of MtrE, trapped an MtrC-MtrE complex with a molecular mass consistent with a stoichiometry of 3:6 (MtrE3MtrC6), suggesting that dimers of MtrC interact with MtrE, presumably by binding to the two grooves. As both MtrE and MtrD are trimeric, our studies suggest that the functional pump is assembled with a stoichiometry of 3:6: