Cong Yao

Biography

CONG Yao is a Professor Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, China. Research Interests: Our research interest is to understand the mechanism of chaperone-assisted protein folding and disaggregation by using electron cryomicroscopy (cryo-EM) single particle and cryotomography techniques, in combination with bioinformatics and flexible fitting tools. Defects in protein folding are associated with a wide variety of human diseases, including cancer and aggregation-linked neurodegenerative diseases such as Huntington’s, Parkinson’s, and Alzheimer’s diseases. Chaperone is a class of proteins which can assist protein folding correctly in the cell. There is a group of oligomeric double-ring chaperones called chaperonin. The eukaryotic chaperonin TRiC/CCT folds ~5-10% of cytosolic proteins including many key structural and regulatory proteins, many of which cannot be folded by any other chaperone. However, little is known about this protein folding nanomachine due to its structural complexity. We focus on the structural mechanisms of how chaperone, such as TRiC/CCT, recognizes its substrate, and how ATP binding and hydrolysis drive its conformational changes and lead to a productive substrate folding. In the long-run, we will extend our study to comprehend how the critical chaperone and its cochaperone cooperate together to assist the protein folding and disaggregation. Another research interest is the image alignment method and modeling tool development and application in cryo-EM data analysis. We have developed a novel FRM2D method for accurate and efficient 2D image alignment in single particle analysis, which has been successfully applied in resolving several subnanometer resolution cryo-EM structures and is available to the fields through EMAN software package.

Research Interest

Our research interest is to understand the mechanism of chaperone-assisted protein folding and disaggregation by using electron cryomicroscopy (cryo-EM) single particle and cryotomography techniques, in combination with bioinformatics and flexible fitting tools. Defects in protein folding are associated with a wide variety of human diseases, including cancer and aggregation-linked neurodegenerative diseases such as Huntington’s, Parkinson’s, and Alzheimer’s diseases. Chaperone is a class of proteins which can assist protein folding correctly in the cell. There is a group of oligomeric double-ring chaperones called chaperonin. The eukaryotic chaperonin TRiC/CCT folds ~5-10% of cytosolic proteins including many key structural and regulatory proteins, many of which cannot be folded by any other chaperone. However, little is known about this protein folding nanomachine due to its structural complexity. We focus on the structural mechanisms of how chaperone, such as TRiC/CCT, recognizes its substrate, and how ATP binding and hydrolysis drive its conformational changes and lead to a productive substrate folding. In the long-run, we will extend our study to comprehend how the critical chaperone and its cochaperone cooperate together to assist the protein folding and disaggregation. Another research interest is the image alignment method and modeling tool development and application in cryo-EM data analysis. We have developed a novel FRM2D method for accurate and efficient 2D image alignment in single particle analysis, which has been successfully applied in resolving several subnanometer resolution cryo-EM structures and is available to the fields through EMAN software package.