Testing the cognitive and the communicative principles of relevance

The article reviews experiments that test consequences of the most central tenets of the theory, namely the cognitive and the communicative principle of relevance

Testing the cognitive and communicative principles of relevance

Outlines basic tenets of relevance theories and presents various experiments providing evidence about these tenet

Delayed cytokinesis generates multinuclearity and potential advantages in the amoeba Acanthamoeba castellanii Neff strain

info:eu-repo/semantics/publishe

How to open the door to System 2: Debiasing the Bat-and-Ball problem

We investigate the empirical conditions under which participants overcome the intuitive and normatively wrong answers they produce in the bat-and-ball problem

Overproduced Brucella abortus PdhS-mCherry forms soluble aggregates in Escherichia coli, partially associating with mobile foci of IbpA-YFP

<p>Abstract</p> <p>Background</p> <p>When heterologous recombinant proteins are produced in <it>Escherichia coli</it>, they often precipitate to form insoluble aggregates of unfolded polypeptides called inclusion bodies. These structures are associated with chaperones like IbpA. However, there are reported cases of "non-classical" inclusion bodies in which proteins are soluble, folded and active.</p> <p>Results</p> <p>We report that the <it>Brucella abortus </it>PdhS histidine kinase fused to the mCherry fluorescent protein forms intermediate aggregates resembling "non-classical" inclusion bodies when overproduced in <it>E. coli</it>, before forming "classical" inclusion bodies. The intermediate aggregates of PdhS-mCherry are characterized by the solubility of PdhS-mCherry, its ability to specifically recruit known partners fused to YFP, suggesting that PdhS is folded in these conditions, and the quick elimination (in less than 10 min) of these structures when bacterial cells are placed on fresh rich medium. Moreover, soluble PdhS-mCherry foci do not systematically colocalize with IpbA-YFP, a marker of inclusion bodies. Instead, time-lapse experiments show that IbpA-YFP exhibits rapid pole-to-pole shuttling, until it partially colocalizes with PdhS-mCherry aggregates.</p> <p>Conclusion</p> <p>The data reported here suggest that, in <it>E. coli</it>, recombinant proteins like PdhS-mCherry may transit through a soluble and folded state, resembling previously reported "non-classical" inclusion bodies, before forming "classical" inclusion bodies. The dynamic localization of IbpA-YFP foci suggests that the IbpA chaperone could scan the <it>E. coli </it>cell to find its substrates.</p