Protein Structural Dynamics
Structural dynamics are essential for understanding every biological mechanism—ranging from chromosome organization and biomolecular phase separation to membrane-protein function—and are the focus of our work in the Protein Structural Dynamics Lab (PSDL).
We employ the novel HS-AFM technique to directly visualize protein movement and dynamics, and complement this with single-molecule approaches such as fluorescence microscopy and magnetic tweezers to probe protein dynamic behaviors.
Chromosome Organization
A chromosome is organized after 2 meters of DNA is replicated and compacted into a chromosome in a living human cell. Each chromosome consists of two sister chromatids, and the two sister chromatids are segregated into two daughter cells to transfer equal amounts of genetic information into two daughter cells. This process is vital for the proliferation and growth of living things. Moreover, this huge amount of DNA is involved in numerous biological processes such as DNA replication, RNA transcription, DNA repair, and chromosome segregation. Therefore, the genome organization in the nucleus should be very precise in 3D space to coordinate cellular processes to prevent any errors in the biological processes. Failure can cause serious diseases such as cancer or developmental disordered diseases. We aim to unravel the molecular mechanism of chromosome organization for various cellular processes by understanding the structural dynamics of chromosomal proteins.
Condensin extrudes DNA loops in steps upto hundreds of base pairs that are generated by ATP binding events
Je-Kyung Ryu#, Sang-Hyun Rah#, Richard Janissen#, Jacob W. Karppenmakers#, and Cees Dekker*, “Condensin extrudes DNA loops in steps upto hundreds of base pairs that are generated by ATP binding events”. Nucleic Acids Research (Impact factor:16.971), gkab1268 (2022).
Structure-function relationships of SMC protein complexes for DNA loop extrusion
Hansol Lee#, Haemin Noh, and Je-Kyung Ryu*, “Structure-function relationships of SMC proteinsfor DNAloop extrusion”, Biodesign, 9(1), 1-13, (2021).
The condensin holocomplex cycles dynamically between open and collapsed states
Je-Kyung Ryu#, Allard Katan, Eli van der Sluis, Thomas Wisse, Jaco van der Torre, Ralph de Groot, Christian Haering, and Cees Dekker*. “The condensin holocomplex cycles dynamically between open and collapsed states”. Nature Structural & Molecular Biology 27(12), 1134-1141(2020).
Intracellular Phase Separation
Phase separation phenomena are involved in myriad biological processes such as chromosome organization, membraneless compartments formation, nuclear pore complex formation, and membrane receptor clusters formation. Generally, phase-separation phenomena in a cell are defined as concentrated nonstoichiometric assemblies of biomolecules that can form via spontaneous or driven processes sharing many of the hallmarks of phase transition. In addition, as gas, liquid, and solid states exist in materials depending on the strength of inter- and intra-molecular interaction, liquid or gel states of biomolecules exist in a living cell. However, what determines the inter- or intramolecular interactions to be a liquid phase or gel phase is not clearly understood in the biological system; hence how the protein interacts together to induce phase separation needs to be understood.
Bridging-induced phase separation induced by cohesin SMC protein complexes
Je-Kyung Ryu#, Celine Bouchoux, Hon Wing Liu, Eugene Kim, Masashi Minamino, Ralph de Groot, AllardKatan, Andrea Bonato, Davide Marenduzzo, Davide Michieletto, Frank Uhlmann*, and Cees Dekker*. “Bridging-induced phase separation induced by cohesin SMC protein complexes”. Science Advances 7(7), abe5905 (2021).
Current Understanding of Molecular Phase Separation in Chromosomes
Je-Kyung Ryu#*, Da-Eun Hwang, and Jeong-Mo Choi*, “Current understandings of molecular phase separation in chromosome”, Int. J. Mol. Sci. 22(19), 10736 (2021).
Membrane proteins
Membrane proteins are a part of or interact with the cell membranes, and approximately 40 % of all cellular proteins reside on lipid membranes, where they play critical roles in metabolic functions and regulating the transfer of information and materials into and out of the cell. Membrane proteins govern many important cellular processes such as nutrient uptake, drug efflux, sensory physiology, immunity, and neuronal communication. It has been widely acknowledged that membrane proteins are also central components in numerous disease states and host-pathogen interactions. Therefore, many membrane proteins are prime drug targets because they perform essential processes in the cell including controlling the flow of information and materials between cells and mediating activities like hormone action and nerve impulses. Therefore, the structural dynamics of membrane proteins is important to lead to new and improved pharmaceutical treatments for a wide range of illnesses such as heart disease, cancer, and infectious diseases.
Models of synaptotagmin-1 to trigger Ca2+-dependent vesicle fusion
Yongsoo Park* and Je-Kyung Ryu*. “Models of synaptotagmin-1 to trigger Ca2+-dependent vesicle fusion”. FEBS Letters 592(21), 3480-3492(2018).
Invited review: Special Issue on “Exocytosis and Endocytosis”, edited by Wilhelm Just
Reconstruction of LPS transfer cascade reveals structural determinants within LBP, CD14 and TLR4-MD2 for efficient LPS recognition and transfer
Je-Kyung Ryu#, Soo Jin Kim#, Sang-Hyun Rah, Ji In Kang, Hi Eun Jung, Heung-Kyu Lee, Jie-Oh Lee, Beom Seok Park, Tae-Young Yoon*, and Ho Min Kim*. “Reconstruction of LPS transfer cascade reveals structural determinants within LBP, CD14 and TLR4-MD2 for efficient LPS recognition and transfer”. Immunity (Impact factor: 31.745) 46(1), 38-50 (2017).
Recommended by F1000, introduced to the magazine of the Science and Technology of KOFST
Progresses in understanding N-ethylmaleimide sensitive factor (NSF) mediated disassembly of SNARE complexes
Je-Kyung Ryu#, Reinhard Jahn*and Tae-Young Yoon*. “Progresses in understanding N-ethylmaleimidesensitive factor (NSF) mediated disassembly of SNARE complexes”. Biopolymers 105(8), 518-531 (2016).
Invited review: Special Issue for GTP and ATP Hydrolysis in Biology, edited by Alfred Wittinghofer.
Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover
Je-Kyung Ryu#, Duyoung Min#, Sang-Hyun Rah#, Soo Jin Kim, Yongsoo Park, Haesoo Kim, Changbong Hyeon, Ho Min Kim, Reinhard Jahn &Tae-Young Yoon. “Spring-loaded unraveling of a single SNARE complex by NSF inone round of ATP turnover”. Science 347(6229), 1485-1489 (2015).