Reconsidering the Carnap-Kuhn Connection

Recently, some philosophers of science (e.g., Gürol Irzik, Michael Friedman) have challenged the ‘received view’ on the relationship between Rudolf Carnap and Thomas Kuhn, suggesting that there is a close affinity (rather than opposition) between their philosophical views. In support of this argument, these authors cite Carnap and Kuhn’s similar views on incommensurability, theory-choice, and scientific revolutions. Against this revisionist view, I argue that the philosophical relationship between Carnap and Kuhn should be regarded as opposed rather than complementary. In particular, I argue that a consideration of the fundamentally disparate nature of the broader philosophical projects of Carnap (logic of science) and Kuhn (providing a theory of scientific revolutions)renders the alleged similarities between their views superficial in comparison to their fundamental differences. In defense of the received view, I suggest that Carnap and Kuhn are model representatives of two contrasting styles of doing philosophy of science, viz., logical analysis and historical analysis respectively. This analysis clarifies the role played by Kuhn’s Structure of Scientific Revolutions in the demise of logical empiricism in the second half of the twentieth-century

The TetR-type transcriptional regulator FasR of Corynebacterium glutamicum controls genes of lipid synthesis during growth on acetate

The addition of fatty acids to either Escherichia coli or Bacillus subtilis elicits an elaborate cellular response of the lipid metabolism. We found that in Corynebacterium glutamicum the expression of accD1 encoding the β-subunit of the essential acetyl-CoA carboxylase is repressed in acetate-grown cells without the addition of fatty acids. The TetR-type transcriptional regulator NCgl2404, termed FasR, was identified and deleted. During growth on acetate, but not on glucose, 17 genes are differentially expressed in the deletion mutant, among them accD1, and fasA and fasB both encoding fatty acid synthases, which were upregulated. Determination of the 5' ends of accD1, fasA, fasB and accBC together with the use of isolated FasR protein identified the FasR binding site, fasO, which is located within the accD1 and fasA transcript initiation site thus blocking transcription by RNA polymerase binding directly. The identified fasO motif is present in C. efficiens or C. diphtheriae, too, and it is actually similarly positioned in these bacteria within the 5' ends of the accD1 and fasA transcripts, and a fasR orthologue is also present. The identification of the FasR-fasO system in Corynebacteriaceae might indicate a conserved transcriptional control of the unique lipid synthesis in these mycolic acid-containing bacteria