232 research outputs found

    Environmental Dilemmas: Ethical Decision Making

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    Publicness as an architectural value

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    That architecture should in some way serve the public good is an idea that mostly goes unquestioned. The corresponding idea that we know who the public is and what its good consists of largely falls apart in the face of even a little probing. This paper investigates the concept of the public inherited from the Enlightenment, its fate in recent times, and possibilities for its reinvention. The argument then goes on to suggest ways in which architecture can have relatively more or less of the quality of publicness

    Architecture, Ethics and the Personhood of Place

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    Dewey and Dancy and the Moral Authority of Rules

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    Pragmatism for architects

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    Serine Phosphorylation of SR Proteins Is Required for Their Recruitment to Sites of Transcription In Vivo

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    Expression of most RNA polymerase II transcripts requires the coordinated execution of transcription, splicing, and 3′ processing. We have previously shown that upon transcriptional activation of a gene in vivo, pre-mRNA splicing factors are recruited from nuclear speckles, in which they are concentrated, to sites of transcription (Misteli, T., J.F. Cáceres, and D.L. Spector. 1997. Nature. 387:523–527). This recruitment process appears to spatially coordinate transcription and pre-mRNA splicing within the cell nucleus. Here we have investigated the molecular basis for recruitment by analyzing the recruitment properties of mutant splicing factors. We show that multiple protein domains are required for efficient recruitment of SR proteins from nuclear speckles to nascent RNA. The two types of modular domains found in the splicing factor SF2/ ASF exert distinct functions in this process. In living cells, the RS domain functions in the dissociation of the protein from speckles, and phosphorylation of serine residues in the RS domain is a prerequisite for this event. The RNA binding domains play a role in the association of splicing factors with the target RNA. These observations identify a novel in vivo role for the RS domain of SR proteins and suggest a model in which protein phosphorylation is instrumental for the recruitment of these proteins to active sites of transcription in vivo
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