Magnetotelluric exploration has shown that the middle and lower crust is anomalously conductive across most of the north-to-south width of the Tibetan plateau. The integrated conductivity (conductance) of the Tibetan crust ranges from 3000 to greater than 20,000 siemens. In contrast, stable continental regions typically exhibit conductances from 20 to 1000 siemens, averaging 100 siemens. Such pervasively high conductance suggests that partial melt and/or aqueous fluids are widespread within the Tibetan crust. In southern Tibet, the high-conductivity layer is at a depth of 15 to 20 kilometers and is probably due to partial melt and aqueous fluids in the crust. In northern Tibet, the conductive layer is at 30 to 40 kilometers and is due to partial melting. Zones of fluid may represent weaker areas that could accommodate deformation and lower crustal flow.
Hsp100 family chaperones of microorganisms and plants cooperate with the Hsp70/Hsp40/NEF system to resolubilize and reactivate stress-denatured proteins. In yeast this machinery also promotes propagation of prions by fragmenting prion polymers. We previously showed the bacterial Hsp100 machinery cooperates with the yeast Hsp40 Ydj1 to support yeast thermotolerance and with the yeast Hsp40 Sis1 to propagate [PSI+] prions. Here we find these Hsp40s similarly directed specific activities of the yeast Hsp104-based machinery. By assessing the ability of Ydj1-Sis1 hybrid proteins to complement Ydj1 and Sis1 functions we show their C-terminal substrate-binding domains determined distinctions in these and other cellular functions of Ydj1 and Sis1. We find propagation of [URE3] prions was acutely sensitive to alterations in Sis1 activity, while that of [PIN+] prions was less sensitive than [URE3], but more sensitive than [PSI+]. These findings support the ideas that overexpressing Ydj1 cures [URE3] by competing with Sis1 for interaction with the Hsp104-based disaggregation machine, and that different prions rely differently on activity of this machinery, which can explain the various ways they respond to alterations in chaperone function.
Known prions (infectious proteins) are self-propagating amyloids or conformationally altered proteins, but in theory an enzyme necessary for its own activation could also be a prion (or a gene composed of protein). We show that yeast protease B is such a prion, called [beta].[beta] is infectious, reversibly curable, and its de novo generation is induced by overexpression of the pro-protease. Present in normal cells but masked by the functionally redundant protease A, [beta] is advantageous during starvation and necessary for sporulation. We propose that other enzymes whose active, modified, form is necessary for their maturation might also be prions.
Using randomized stimulus onset asynchrony (SOAs), the authors traced the time course of Stroop interference and facilitation in normal participants and participants with schizophrenia. Unlike earlier findings using blocked SOAs, singular peaks in interference, facilitation, or both occurred at particular SOAs. The peaks of normal participants and participants with schizophrenia differed. Findings are congruent with a model of Stroop performance that posits individual differences in processing speeds of target and nontarget stimulus dimensions, coupled with critical points in response selection. Participants with schizophrenia also showed more overall interference than normal control participants. A second experiment that added a temporal gap between the distractor word and target color obliterated Stroop effects only for individuals with schizophrenia. These findings provide a new empirical basis for models of Stroop effects. They are also consistent with hypotheses about the importance of the prefrontal cortex for working memory and prefrontal dysfunction in schizophrenia.
Human chaperone DnaJB6, an Hsp70 co-chaperone whose defects cause myopathies, protects cells from polyglutamine toxicity and prevents purified polyglutamine and Aβ peptides from forming amyloid. Yeast prions [URE3] and [PSI(+)] propagate as amyloid forms of Ure2 and Sup35 proteins, respectively. Here we find DnaJB6-protected yeast cells from polyglutamine toxicity and cured yeast of both [URE3] prions and weak variants of [PSI(+)] prions but not strong [PSI(+)] prions. Weak and strong variants of [PSI(+)] differ only in the structural conformation of their amyloid cores. In line with its anti-prion effects, DnaJB6 prevented purified Sup35NM from forming amyloids at 37 °C, which produce predominantly weak [PSI(+)] variants when used to infect yeast, but not at 4 °C, which produces mostly strong [PSI(+)] variants. Thus, structurally distinct amyloids composed of the same protein were differentially sensitive to the anti-amyloid activity of DnaJB6 both in vitro and in vivo. These findings have important implications for strategies using DnaJB6 as a target for therapy in amyloid disorders.
Two negative priming experiments in older and younger adults are reported. Participants in Experiment 1, involving both positive and negative priming conditions, showed both types of priming. There were no significant differences between age groups. If anything, older participants showed more negative priming. In Experiment 2, involving only negative priming conditions, similar results were obtained. Our findings rule out possible effects of experimental conditions that episodic retrieval theorists have suggested might account for negative priming in older adults. Although our results may be consistent with an explanation of negative priming in older adults by an expansively specified theory of episodic retrieval, they are at least as consistent with the view that inhibitory processes are intact in older adults. In light of these findings, conflicting empirical results and alternative views of negative priming in older adults are examined.
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