Campañas medioambientales contra empresas forestales: ¿Cuál es el objetivo de estas campañas?

Campaigns by environmental non-governmental organisations (ENGOs) can have far reaching consequences in determining the policies of governments and corporations. This paper examines campaigns targeting forestry companies to determine what makes a successful campaign. Over forty ENGOs completed a questionnaire defining what they perceive to constitute a successful campaign. The responses were analysed using Analytical Hierarchy Process. The results showed that campaigns by ENGOs have two main targets: changes in laws and the target group implementing the campaign’s recommendation(s). Achieving these targets, for most, constitute a successful campaign. Subsequently, representatives of seven ENGOs were questioned to attain their perspectives of the results in comparison to campaigns they are conducting against forest enterprises. They supported the results of the questionnaire, but also felt that there are various other factors that need to be considered (e.g. the campaign’s timeframe and the possibility of having hidden targets) that increase the issue’s complexity.Campañas llevadas a cabo por organizaciones no gubernamentales ambientalistas (ONGsA) pueden tener importantes consecuencias a la hora de influenciar las políticas tanto de gobiernos como de corporaciones industriales. Este artículo se centra en el estudio de campañas cuyo blanco son las empresas madereras, analizando que condiciones deben cumplir dichas campañas para poder ser consideradas como exitosas. Para ello, más de cuarenta ONGsA rellenaron un cuestionario en el que se les pedía que indicaran su opinión sobre que define una campaña exitosa. Las respuestas fueron analizadas utilizando un Proceso Analítico Jerárquico (AHP). Los resultados mostraron que las campañas de las ONGsA tienen dos objetivos principales, obtener cambios en las leyes y que la compañía o gobierno objetivo de la campaña cumpla las recomendaciones propuestas. A posteriori, los representantes de siete ONGsA, con campañas ambientales en curso contra empresas madereras, fueron preguntados sobre si los resultados obtenidos a través del análisis AHP estaban en concordancia con las perspectivas para sus campañas ambientales. Como resultado, se obtuvo que si bien sus perspectivas coincidían con los resultados del análisis, existen otros factores a tener en cuenta (por ejemplo el marco temporal de la campaña y la posibilidad de afectar objetivos no explícitamente señalados) que aumentan la complejidad del problema

slpM, a gene coding for an "S-layer-like array" overexpressed in S-layer mutants of Thermus thermophilus HB8.

S-layer deletion mutants of Thermus thermophilus HB8 overproduce a regular array which surrounds groups of several cells. Averages of two-dimensional projections revealed a detailed architecture similar in general morphology and unit cell dimensions to that of the S-layer but having a different mass distribution. The structural components of these "S-layer-like arrays" are a group of three proteins of 52 (P52), 50 (P50), and 36 (P36) kDa, which are overexpressed in S-layer mutants. These three proteins specifically bind antibodies against P52, suggesting that the smaller proteins correspond to fragments derived from P52. This hypothesis was demonstrated by the identity of the trypsin digestion products of P52 and P50. The gene slpM, responsible for the synthesis of P52, was cloned by using synthetic oligonucleotides designed from partial amino acid sequences of P52 and P50. When slpM was expressed in Escherichia coli, proteins specifically recognized by anti-P52 antiserum whose electrophoretic mobilities were similar to those of P52 and P36 were detected. The sequence of slpM revealed the existence of an open reading frame in which the amino termini of P52, P50, and P36 were identified. The unprocessed product of slpM is a 469-amino-acid-long polypeptide whose theoretical M(r) (52,131) was in good agreement with the electrophoretic mobility of P52. The properties deduced for the product of slpM are very different from those of any S-layer protein so far sequenced. The possible roles of SlpM in wild-type cells are discussed