Guillermo Gómez-Peña : a "new age shaman” in a bohemian theme park

The Marquis de Sade was declared, “the fist commandment of art is ‘never to bore,’” and perhaps no other artist of his generation has embodied this sentiment more than Guillermo Gómez- Peña, the Mexican-born performance artist and cultural theorist living in San Francisco. Since the early 1980s Gómez-Peña, along with his performance troupe La Pocha Nostra, have been engaged in “reverse anthropology” staging “postcolonial” performances that foreground race and intervene in our cultural fears and desires by focusing on our obsession with the exotic. He deftly navigates the “post-multicultural” world – accelerated by globalization and nation branding – by using elaborate performative and interactive elements that expose (to the audience) their deeply embedded cultural stereotypes and desires for the other.

Néstor-Guillermo Progeria Syndrome: a biochemical insight into Barrier-to-Autointegration Factor 1, alanine 12 threonine mutation

Background Premature aging syndromes recapitulate many aspects of natural aging and provide an insight into this phenomenon at a molecular and cellular level. The progeria syndromes appear to cause rapid aging through disruption of normal nuclear structure. Recently, a coding mutation (c.34G > A [p.A12T]) in the Barrier to Autointegration Factor 1 (BANF1) gene was identified as the genetic basis of Néstor-Guillermo Progeria syndrome (NGPS). This mutation was described to cause instability in the BANF1 protein, causing a disruption of the nuclear envelope structure. Results Here we demonstrate that the BANF1 A12T protein is indeed correctly folded, stable and that the observed phenotype, is likely due to the disruption of the DNA binding surface of the A12T mutant. We demonstrate, using biochemical assays, that the BANF1 A12T protein is impaired in its ability to bind DNA while its interaction with nuclear envelope proteins is unperturbed. Consistent with this, we demonstrate that ectopic expression of the mutant protein induces the NGPS cellular phenotype, while the protein localizes normally to the nuclear envelope. Conclusions Our study clarifies the role of the A12T mutation in NGPS patients, which will be of importance for understanding the development of the disease.