This article addresses these shortcomings by studying politicians' personalization, not as a product of media logic but by looking at politicians' media-related practices and the media's anchoring of practices. Our in-depth interviews with Flemish politicians show that politicians' practices are in many ways organized by the media, but at the same time aim to retain control over them. Practices related to image-building and the constitution of the private-public boundary demonstrate this. We conclude that practice theory offers great potential for mediatization research but needs further empirical application.

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This article brings a synthesis of the recent literature about the role the media have played in the transformation of the public sphere. Departing from this literature, a general research framework for a critical political economy of the public sphere is presented. The central thesis of this approach is that a political economy of the public sphere should not be restricted to an analysis of its institutional configuration and the actual labour process, but must extend its radius of action from the production of media messages to a political economy of reception and its signification.

Fanconi anemia is a chromosomal breakage disorder with eight complementation groups (A-H), and three genes (FANCA, FANCC, and FANCG) have been identified. Initial investigations of the interaction between FANCA and FANCC, principally by co-immunoprecipitation, have proved controversial. We used the yeast two-hybrid assay to test for interactions of the FANCA, FANCC, and FANCG proteins. No activation of the reporter gene was observed in yeast co-expressing FANCA and FANCC as hybrid proteins, suggesting that FANCA does not directly interact with FANCC. However, a high level of activation was found when FANCA was co-expressed with FANCG, indicating strong, direct interaction between these proteins. Both FANCA and FANCG show weak but consistent interaction with themselves, suggesting that their function may involve dimerisation. The site of interaction of FANCG with FANCA was investigated by analysis of 12 mutant fragments of FANCG. Although both N- and C-terminal fragments did interact, binding to FANCA was drastically reduced, suggesting that more than one region of the FANCG protein is required for proper interaction with FANCA.

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