期刊
BMB REPORTS
卷 50, 期 9, 页码 478-483出版社
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
DOI: 10.5483/BMBRep.2017.50.9.084
关键词
Fluorescence cross-correlation spectroscopy; Live cell; Protein interaction; Remodeling factors; Yeast prions
资金
- National Institutes of Health Grant [GM53655]
- USDA Cooperative State Research, Education and Extension Service (CSREES) [WISO4769]
- Human Frontier Science Program Long-Term Fellowship
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM053655] Funding Source: NIH RePORTER
Budding yeast has dozens of prions, which are mutually dependent on each other for the de novo prion formation. In addition to the interactions among prions, transmissions of prions are strictly dependent on two chaperone systems: the Hsp104 and the Hsp70/Hsp40 (J-protein) systems, both of which cooperatively remodel the prion aggregates to ensure the multiplication of prion entities. Since it has been postulated that prions and the remodeling factors constitute complex networks in cells, a quantitative approach to describe the interactions in live cells would be required. Here, the researchers applied dual-color fluorescence cross-correlation spectroscopy to investigate the molecular network of interaction in single live cells. The findings demonstrate that yeast prions and remodeling factors constitute a network through heterogeneous protein-protein interactions.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据