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Zhong Z.,Liaoning University | Zhong Z.,Chengde Petroleum College | Wang L.,Liaoning University | Xie H.,Chengde Petroleum College | And 6 more authors.
Shengwu Gongcheng Xuebao/Chinese Journal of Biotechnology | Year: 2012

In order to quantify the curing effects of phenanthridine on yeast prion, we introduced semi-denaturing agarose gel electrophoresis and fluorescence recovery after photobleaching techniques to quantify the curing effects of phenanthridine on yeast prion at the protein and cellular levels with the [PSI+] yeast strain expressing GFP-Sup35p (NGMC). The results showed that these two approaches could precisely quantify the curing effects of phenanthridine on [PSI+] cells. After a treatment for 1 through 5 days with phenanthridine, the curing rates of [PSI+] cells were 0%, 0%, 51.7%, 87.5% and 94.4%, respectively. Meanwhile, we quantified the sizes of Sup35p polymers in phenanthridine induced pink phenotype cells. The aggregation status in 1-2 days phenanthridine treated cells were similar to those in [PSI+] cells, while the aggregation status in 3-5 days phenanthridine treated cells were similar to those in [psi-] cells.


Yu A.,Liaoning University | Wang Y.,Province Key Laboratory of Animal Resource and Epidemic Disease Prevention | He J.,Liaoning University | He J.,Province Key Laboratory of Animal Resource and Epidemic Disease Prevention | And 6 more authors.
Journal of Biomolecular Structure and Dynamics | Year: 2010

Chicken cystatin variant I108T is a mutant in the hydrophobic core of the molecule. It has shown many amyloid-prone characteristics in our previous experimental study. To explore the detailed structural and dynamic properties of the amyloidogenic mutant I108T, 10 ns molecular dynamic simulations of the I108T mutant and wild-type chicken cystatins were performed in this study. Our results suggested that the I108T mutant, which exhibited larger secondary structural fluctuations and hydrophobic core expanding tendency compared with the wild-type chicken cystatin, is a new amyloidogenic form of chicken cystatin, and therefore supported the hypothesis to some extent that site mutations in the hydrophobic core might induce the domain swapping. ©Adenine Press (2010).


Song Y.,Liaoning University | Lan W.,Liaoning University | Wu X.,Liaoning University | He J.,Liaoning University | And 5 more authors.
Protein and Peptide Letters | Year: 2010

[PSI+] phenotype can be transiently induced when Magnesium chloride (MgCl2) was the selective pressure in SUP35 repeat-expansion mutant [psī] yeast strains. We further investigated [PSI+] phenotype change under different MgCl2 conditions with native Sup35p and quantified the Sup35p status changes with fluorescence recovery after pho-tobleaching (FRAP) and semi-denaturing detergent-agarose gel electrophoresis (SDD-AGE) analysis. It was found that the [PSI+] phenotype presented a dose-dependent relationship with the concentrations of MgCl2. Furthermore, Sup35p aggregated in MgCl2 treated cells but did not form large aggregates as it does in [PSI+] cells, and the size of Sup35p aggregates showed a time-dependent relationship with the MgCl2 application. The aggregation of Sup35p strictly depended on the presence of MgCl2 stress in our strains. © 2010 Bentham Science Publishers Ltd.

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