Bio

Bio


Jinglong was trained in a single-molecule lab in Institute Jacques Monod and École Normale Supérieure Paris and obtained his PhD degree from University of Paris in 2019, France. He dissected the molecular machinery of human and bacterial Non-homologous end joining, and interrogated the mechanism of SpCas9 plasticity on targeting DNA with deviant PAMs using single-molecule nanomanipulation tools. Jinglong joined the Frock lab in Jan 2020, and he is working on DSB-related chromosome topological changes and genomic interactions.

Stanford Advisors


Patents


  • Terence Strick, Charlie Grosse, Dorota Kostrz, Jinglong Wang, Marc Nadal. "France Patent 1762848 Molecule d'ADN Double- Brin pour la Detection et la Caracterisation des Interactions Moleculaires", CNRS, Dec 21, 2018

Publications

All Publications


  • A Modular DNA Scaffold to Study Protein-Protein Interactions at Single-Molecule Resolution Kostrz, D. N., Wayment-Steele, H. K., Wang, J., Follenfant, M., Pande, V. S., Triller, A., Specht, C. G., Strick, T. R., Gosse, C. CELL PRESS. 2020: 187A
  • A modular DNA scaffold to study protein-protein interactions at single-molecule resolution. Nature nanotechnology Kostrz, D., Wayment-Steele, H. K., Wang, J. L., Follenfant, M., Pande, V. S., Strick, T. R., Gosse, C. 2019

    Abstract

    The residence time of a drug on its target has been suggested as a more pertinent metric of therapeutic efficacy than the traditionally used affinity constant. Here, we introduce junctured-DNA tweezers as a generic platform that enables real-time observation, at the single-molecule level, of biomolecular interactions. This tool corresponds to a double-strand DNA scaffold that can be nanomanipulated and on which proteins of interest can be engrafted thanks to widely used genetic tagging strategies. Thus, junctured-DNA tweezers allow a straightforward and robust access to single-molecule force spectroscopy in drug discovery, and more generally in biophysics. Proof-of-principle experiments are provided for the rapamycin-mediated association between FKBP12 and FRB, a system relevant in both medicine and chemical biology. Individual interactions were monitored under a range of applied forces and temperatures, yielding after analysis the characteristic features of the energy profile along the dissociation landscape.

    View details for DOI 10.1038/s41565-019-0542-7

    View details for PubMedID 31548690

  • Dissection of DNA double-strand-break repair using novel single-molecule forceps. Nature structural & molecular biology Wang, J. L., Duboc, C., Wu, Q., Ochi, T., Liang, S., Tsutakawa, S. E., Lees-Miller, S. P., Nadal, M., Tainer, J. A., Blundell, T. L., Strick, T. R. 2018; 25 (6): 482–87

    Abstract

    Repairing DNA double-strand breaks (DSBs) by nonhomologous end joining (NHEJ) requires multiple proteins to recognize and bind DNA ends, process them for compatibility, and ligate them together. We constructed novel DNA substrates for single-molecule nanomanipulation, allowing us to mechanically detect, probe, and rupture in real-time DSB synapsis by specific human NHEJ components. DNA-PKcs and Ku allow DNA end synapsis on the 100 ms timescale, and the addition of PAXX extends this lifetime to ~2 s. Further addition of XRCC4, XLF and ligase IV results in minute-scale synapsis and leads to robust repair of both strands of the nanomanipulated DNA. The energetic contribution of the different components to synaptic stability is typically on the scale of a few kilocalories per mole. Our results define assembly rules for NHEJ machinery and unveil the importance of weak interactions, rapidly ruptured even at sub-picoNewton forces, in regulating this multicomponent chemomechanical system for genome integrity.

    View details for DOI 10.1038/s41594-018-0065-1

    View details for PubMedID 29786079

    View details for PubMedCentralID PMC5990469

  • The histone H3.3K36M mutation reprograms the epigenome of chondroblastomas. Science (New York, N.Y.) Fang, D., Gan, H., Lee, J. H., Han, J., Wang, Z., Riester, S. M., Jin, L., Chen, J., Zhou, H., Wang, J., Zhang, H., Yang, N., Bradley, E. W., Ho, T. H., Rubin, B. P., Bridge, J. A., Thibodeau, S. N., Ordog, T., Chen, Y., van Wijnen, A. J., Oliveira, A. M., Xu, R. M., Westendorf, J. J., Zhang, Z. 2016; 352 (6291): 1344–48

    Abstract

    More than 90% of chondroblastomas contain a heterozygous mutation replacing lysine-36 with methionine-36 (K36M) in the histone H3 variant H3.3. Here we show that H3K36 methylation is reduced globally in human chondroblastomas and in chondrocytes harboring the same genetic mutation, due to inhibition of at least two H3K36 methyltransferases, MMSET and SETD2, by the H3.3K36M mutant proteins. Genes with altered expression as well as H3K36 di- and trimethylation in H3.3K36M cells are enriched in cancer pathways. In addition, H3.3K36M chondrocytes exhibit several hallmarks of cancer cells, including increased ability to form colonies, resistance to apoptosis, and defects in differentiation. Thus, H3.3K36M proteins reprogram the H3K36 methylation landscape and contribute to tumorigenesis, in part through altering the expression of cancer-associated genes.

    View details for DOI 10.1126/science.aae0065

    View details for PubMedID 27229140

    View details for PubMedCentralID PMC5460624

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