Speaker：Ke Tan (谭轲) Jingjing Liu (刘菁菁) Jingrou Li (李婧柔)

Time：15:00 - 18:00

Abstract:

Hsp90 (Heat shock protein 90) is a family member of chaperone which has two opposite effects on its target proteins when the target proteins mutated. Under the guidance of Hsp90, sometimes the mutated target proteins can fold and function normally, hiding the mutations and preventing the mutations from natural selections. However, the mutated target proteins can also fold in a totally different way with the help of Hsp90 and generate novel functions, which will affect the natural selection on the mutated proteins. Another example of this protein-level phenotype-selection is the  prion, which shows us the underlying relationship between protein folding and evolution. In this journal club, by focusing on Hsp90 and prion, we will review and discuss studies about the effects of protein folding on natural selection and evolution.

Guest information:

1. Dr. Zengyi Chang (PKU)

http://bio.pku.edu.cn/en/teacher_dis.php?cid=204&&teaid=11

Recommend Literatures：

Review:

1. Jarosz, Daniel F., Mikko Taipale, and Susan Lindquist. "Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms." Annual review of genetics 44 (2010): 189-216.

Link: https://www.annualreviews.org/doi/abs/10.1146/annurev.genet.40.110405.090412

Papers:

1. Cowen, Leah E., and Susan Lindquist. "Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi." Science 309.5744 (2005): 2185-2189.

Link: http://science.sciencemag.org/content/309/5744/2185

2. Rohner, Nicolas, et al. "Cryptic variation in morphological evolution: HSP90 as a capacitor for loss of eyes in cavefish." Science 342.6164 (2013): 1372-1375.

Link: http://science.sciencemag.org/content/342/6164/1372