LaTBP1: A Leishmania amazonensis DNA-binding protein that associates in vivo with telomeres and GT-rich DNA using a Myb-like domain

Different species of Leishmania can cause a variety of medically important diseases, whose control and treatment are still health problems. Telomere binding proteins (TBPs) have potential as targets for anti-parasitic chemotherapy because of their importance for genome stability and cell viability. Here, we describe LaTBP1 a protein that has a Myb-like DNA-binding domain, a feature shared by most double-stranded telomeric proteins. Binding assays using full-length and truncated LaTBP1 combined with spectroscopy analysis were used to map the boundaries of the Myb-like domain near to the protein only tryptophan residue. The Myb-like domain of LaTBP1 contains a conserved hydrophobic cavity implicated in DNA-binding activity. A hypothetical model helped to visualize that it shares structural homology with domains of other Myb-containing proteins. Competition assays and chromatin immunoprecipitation confirmed the specificity of LaTBP1 for telomeric and GT-rich DNAs, suggesting that LaTBP1 is a new TBP. (C) 2007 Elsevier B.V. All rights reserved.

The Saccharomyces cerevisiae COQ10 gene encodes a START domain protein required for function of coenzyme Q in respiration

Deletion of the Saccharomyces cerevisiae gene YOL008W, here referred to as COQ10, elicits a respiratory defect as a result of the inability of the mutant to oxidize NADH and succinate. Both activities are restored by exogenous coenzyme Q(2). Respiration is also partially rescued by COQ2, COQ7, or COQ8/ABC1, when these genes are present in high copy. Unlike other coq mutants, all of which lack Q(6), the coq10 mutant has near normal amounts of Q(6) in mitochondria. Coq10p is widely distributed in bacteria and eukaryotes and is homologous to proteins of the aromatic-rich protein family Pfam03654 and to members of the START domain superfamily that have a hydrophobic tunnel implicated in binding lipophilic molecules such as cholesterol and polyketides. Analysis of coenzyme Q in polyhistidine-tagged Coq10p purified from mitochondria indicates the presence 0.032-0.034 mol of Q(6)/mol of protein. We propose that Coq10p is a Q(6)-binding protein and that in the coq10 mutant Q(6) it is not able to act as an electron carrier, possibly because of improper localization.

Genomic Strategy Identifies a Missense Mutation in WD-Repeat Domain 65 (WDR65) in an Individual With Van der Woude Syndrome

Genetic variation in the transcription factor interferon regulatory factor 6 (IRF6) causes and contributes risk for oral clefting disorders. We hypothesized that genes regulated by IRF6 are also involved in oral clefting disorders. We used five criteria to identify potential IRF6 target genes; differential gene expression in skin taken from wild-type and Irf6-deficient murine embryos, localization to the Van der Woude syndrome 2 (VWS2) locus at 1p36-1p32, overlapping expression with Irf6, presence of a conserved predicted-binding site in the promoter region, and a mutant murine phenotype that was similar to the Irf6 mutant mouse. Previously, we observed altered expression for 573 genes; 13 were located in the murine region syntenic to the VWS2 locus. Two of these genes, Wdr65 and Stratifin, met 4 of 5 criteria. Wdr65 was a novel gene that encoded a predicted protein of 1,250 amino acids with two WD domains. As potential targets for Irf6 regulation, we hypothesized that disease-causing mutations will be found in WDR65 and Stratifin in individuals with VWS or VWS-like syndromes. We identified a potentially etiologic missense mutation in WDR65 in a person with VWS who does not have an exonic mutation in IRF6. The expression and mutation data were consistent with the hypothesis that WDR65 was a novel gene involved in oral clefting. (C) 2011 Wiley-Liss, Inc.

Amphibians and reptiles from a highly diverse area of the Caatinga domain: composition and conservation implications

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Mutational analysis of the GAP-related domain of the neurofibromatosis type 1 gene in Brazilian NF1 patients

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

DODAB and DODAC bilayer-like aggregates in the micromolar surfactant concentration domain

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

The two-loop massless (lambda/4!)phi(4) model in nontranslational invariant domain

We study the (lambda/4!)phi(4) massless scalar field theory in a four-dimensional Euclidean space, where all but one of the coordinates are unbounded. We are considering Dirichlet boundary conditions in two hyperplanes, breaking the translation invariance of the system. We show how to implement the perturbative renormalization up to two-loop level of the theory. First, analyzing the full two and four-point functions at the one-loop level, we show that the bulk counterterms are sufficient to render the theory finite. Meanwhile, at the two-loop level, we must also introduce surface counterterms in the bare Lagrangian in order to make finite the full two and also four-point Schwinger functions. (c) 2006 American Institute of Physics.

Relics of eclogite facies assemblages in the Ceara Central Domain, NW Borborema Province, NE Brazil: Implications for the assembly of West Gondwana

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Exponential decay for Kirchhoff wave equation with nonlocal condition in a noncylindrical domain

In this paper, we prove the exponential decay as time goes to infinity of regular solutions of the problem for the Kirchhoff wave equation with nonlocal condition and weak dampingu(tt) - M (\\delU\\(2)(2)) Deltau + integral(0)(t) g(t - s)Deltau(.,s) ds + alphau(t) = 0, in (Q) over cap,where (Q) over cap is a noncylindrical domain of Rn+1 (n greater than or equal to 1) with the lateral boundary (&USigma;) over cap and alpha is a positive constant. (C) 2004 Elsevier Ltd. All rights reserved.

Computational studies of the reversible domain swapping of p13suc1

A minimalist representation of protein structures using a Go- like potential for interactions is implemented to investigate the mechanisms of the domain swapping of p13suc1, a protein that exists in two native conformations: a monomer and a domain- swapped dimer formed by the exchange of a beta- strand. Inspired by experimental studies which showed a similarity of the transition states for folding of the monomer and the dimer, in this study we justify this similarity in molecular descriptions. When intermediates are populated in the simulations, formation of a domain- swapped dimer initiates from the ensemble of unfolded monomers, given by the fact that the dimer formation occurs at the folding/ unfolding temperature of the monomer ( T-f). It is also shown that transitions, leading to a dimer, involve the presence of two intermediates, one of them has a dimeric form and the other is monomeric; the latter is much more populated than the former. However, at temperatures lower than T-f, the population of intermediates decreases. It is argued that the two folded forms may coexist in absence of intermediates at a temperature much lower than T-f. Computational simulations enable us to find a mechanism, `` lock- and- dock'', for domain swapping of p13suc1. To explore the route toward dimer formation, the folding of unstructured monomers must be retarded by first locking one of the free ends of each chain. Then, the other free termini could follow and dock at particular regions, where most intrachain contacts are formed, and thus de. ne the transition states of the dimer. The simulations also showed that a decrease in the maximum distance between monomers increased their stability, which is explained based on confinement arguments. Although the simulations are based on models extracted from the native structure of the monomer and the dimer of p13suc1, the mechanism of the domain- swapping process could be general, not only for p13suc1.

Exact boundary control for the wave equation in a polyhedral time-dependent domain

We establish exact boundary controllability for the wave equation in a polyhedral domain where a part of the boundary moves slowly with constant speed in a small interval of time. The control on the moving part of the boundary is given by the conormal derivative associated with the wave operator while in the fixed part the control is of Neuman type. For initial state H-1 x L-2 we obtain controls in L-2. (C) 1999 Elsevier B.V. Ltd. All rights reserved.

Does 75% of the difference between VO2 at lactate threshold and VO2max lie at the severe-intensity domain in well-trained cyclists?

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Study on suppression of otoacoustic emissions: lateral domain

A pon stimulation by contralateral, ipsilateral or bilateral noise, the medial olivocochlear efferent tract changes the amplitude of otoacoustic emissions relative to the tested ear, reducing or removing it; this resulted in a reduction/suppression effect of otoacoustic emissions. Differences in patterns of elimination/reduction of otoacoustic emissions between ears have been documented worldwide; there are, however, no Brazilian studies investigating the effect of lateral dominance.Aims: To compare the effect of the presence of deletion/reduction of otoacoustic emissions and their amplitude relative to lateral dominance in normal hearing adults.Methods: A clinical and experimental study. The sample comprised 75 individuals. The methodology was conventional - linear click intensity of 60 dB SPL; white noise was contralateral stimulation at 60 dB SPL.Description of results: There were no statistically significant differences between right and left ear results, in terms of asymmetry of the degree of otoacoustic emissions and the presence of suppression/reduction.Conclusion: There is no lateral dominance in the degree of otoacoustic emissions in the presence of suppression/reduction in the study population.