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A new species of Liolaemus is described from southwest of the town of Añelo, Neuquén Province, Argentina. Integrative evidence methodology of external morphological characters and molecular phylogenetic analyses of mitochondrial DNA (cyt-b) is used to place the new species to the species group of Liolaemus boulengeri. The new species is phenotypically close to L. mapuche. The new Liolaemus is medium to large in size (males 77.64–83.98 mm, females 72.88–78.58 mm), with evident sexual dichromatism. Genetic distances of the mtDNA (cyt-b) between the new species and its closest relative species are greater than 3% (L. cuyanus 7.48–12.02%; L. josei 7.56–9.60%; L. puelche 8.23–9.93%; L. mapuche 8.51–9.79%). Molecular and morphological phylogenetic results show L. mapuche as the sister species of the new one. The new species is larger than L. mapuche. Dorsal and ventral scales are more numerous in the new species than in L. mapuche, precloacal pores in females are present in L. mapuche and absent in the new species. It has strict psammophilic habits, using sand mounds and sheltering, under Alpataco (Neltuma alpataco) bushes. The L. boulengeri group now contains 75 species distributed in Argentina, Bolivia, Brazil, Chile, Paraguay, Peru and Uruguay.
Requirements for the interaction of mouse Polkappa with ubiquitin and its biological significance
(2008)
Polkappa protein is a eukaryotic member of the DinB/Polkappa branch of the Y-family DNA polymerases, which are involved in the tolerance of DNA damage by replicative bypass. Despite universal conservation through evolution, the precise role(s) of Polkappa in this process has remained unknown. Here we report that mouse Polkappa can physically interact with ubiquitin by yeast two-hybrid screening, glutathione S-transferase pulldown, and immunoprecipitation methods. The association of Polkappa with ubiquitin requires the ubiquitin-binding motifs located at the C terminus of Polkappa. In addition, Polkappa binds with monoubiquitinated proliferating cell nuclear antigen (PCNA) more robustly than with non-ubiquitinated PCNA. The ubiquitin-binding motifs mediate the enhanced association between monoubiquitinated PCNA and Polkappa. The ubiquitin-binding motifs are also required for Polkappa to form nuclear foci after UV radiation. However, the ubiquitin-binding motifs do not affect Polkappa half-life. Finally, we have examined levels of Polkappa expression following the exposure of mouse cells to benzo[a]pyrene-dihydrodiol epoxide or UVB radiation.
Protein post-translational modification with ubiquitin (Ub) is a versatile signal regulating almost all aspects of cell biology, and an increasing range of diseases is associated with impaired Ub modification. In this light, the Ub system offers an attractive, yet underexplored route to the development of novel targeted treatments. A promising strategy for small molecule intervention is posed by the final components of the enzymatic ubiquitination cascade, E3 ligases, as they determine the specificity of the protein ubiquitination pathway. Here, we present UbSRhodol, an autoimmolative Ub-based probe, which upon E3 processing liberates the pro-fluorescent dye, amenable to profile the E3 transthiolation activity for recombinant and in cell-extract E3 ligases. UbSRhodol enabled detection of changes in transthiolation efficacy evoked by enzyme key point mutations or conformational changes, and offers an excellent assay reagent amenable to a high-throughput screening setup allowing the identification of small molecules modulating E3 activity.