Lingling Chen
Associate Professor, Molecular and Cellular Biochemistry Department
Education
Ph.D., Stanford University, 1996
Research
Structural and biochemical studies on protein-protein interactions in GroEL-mediated protein folding and microbial communications.
Representative Publications
Zhida Zheng, Clay Fuqua, and Lingling Chen. The binding site of DNA on quorum-sensing transcript factor TraR does not overlap with that of the Anti-Activator. Submitted to Biochem. Biophys. Res. Commun. 2012, in press
Zhida Zheng, Dejian Ma, Timothy Yahr, and Lingling Chen. The Transiently Ordered Regions in Intrinsically Disordered ExsE Are Correlated with Structural Elements Involved in Chaperone Binding. Biochem. Biophys. Res. Commun. Nov.25, 2011 (Epub)
Yi Pan, Valena Fiscus, Wuyi Meng, Zhida Zheng, Lianhui Zhang, Clay Fuqua, and Lingling Chen. The Agobacterium tumefaciens Transcriptional Factor BlcR Is Regulated via Oligomerization. J. Biol. Chem. 286: 20431-40, 2011
Melissa Illingworth, Andrew Ramsey, Zhida Zheng, and Lingling Chen. Stimulating the substrate folding activity of a single-ring GroEL variant by modulating the cochaperonin GroES. J. Biol. Chem. 286: 30401-8, 2011
Zhida Zheng, Dejian Ma, Timothy Yahr, and Lingling Chen. The Transiently Ordered Regions in Intrinsically Disordered ExsE Are Correlated with Structural Elements Involved in Chaperone Binding. Biochem. Biophys. Res. Commun. In press, 2011
Mair Churchill and Lingling Chen. Structural Basis of Acyl-homoserine Lactone-Dependent Signaling. Chem. Rev. 111: 68-85, 2011
Li, Y., Zheng, Z., Ramsey, A., and Chen, L. 2010. Analysis of peptides and proteins in their binding to GroEL. Journal of Peptide Science 16 (12): 693- 700.
Chen, L. 2010. Signal synthesis for a rapid response. Structure 18 (9): 1072- 1073.
Li, Y. Gao, X., and Chen, L. 2009. GroEL recognizes an amphipathic helix and binds to the hydrophobic side. Journal of Biological Chemistry 284 (7): 4324–4331.
Yali Li, Xinfeng Gao, Lingling Chen. GroEL recognizes an amphipathetic helix and binds to the hydrophobic side, accepted by J. Biol. Chem. 2008
Guozhou Chen, Phillip Jeffery, Clay Fuqua, Yigong Shi and Lingling Chen. Structural basis of TraM anti-activation of quorum sensing transcription factor TraR. Proc. Natl. Acad. Sci. USA, 104:16474-16479, 2007.
Banga, S., Gao, P., Shen, X., Fiscus, V., Zong, W., Chen, L., and Luo, Z. Legionella pneumophila inhibits macrophage apoptosis by targeting pro-death members of the Bcl2 protein family. Proc. Natl. Acad. Sci. USA 104:5121-5126, 2007.
Zhida Zheng, Guozhou Chen, Evan D. Brutinel, Timothy L. Yahr, and Lingling Chen. Biochemical characterization of a regulatory cascade controlling transcription of the Pseudomonas aeruginosa type III secretion system. J. Biol. Chem. 282:6136-6142, 2007.
Guozhou Chen, Chao Wang, Clay Fuqua, Lian-Hui Zhang and Lingling Chen. The crystal structure and mechanism of TraM2, a second quorum sensing
antiactivator of Agrobacterium tumefaciens strain A6. J. Bact. 188:8244-8251, 2006.
Lykken, G., Chen, G., Brutinel, E., Chen, L., and Yahr, T. Characterization of ExsC and ExsD self-association and heterocomplex formation. J. Bact. 188:6832-6840, 2006.
Wang, C., Zhang, H.-B., Chen, G., Chen, L, and Zhang, L.-H.. Dual Control of Quorum Sensing by Two TraM-Type Antiactivators in Agrobacterium tumefaciens Octopine Strain A6. Journal of Bacteriology, April 2006, p. 2435-2445, Vol. 188, No. 7
Chen, G., Malenkos, J., Cha, M., Fuqua, C. and Chen, L. 2004. Quorum-Sensing Antiactivator TraM Forms a Dimer That Dissociates to Inhibit TraR. Molecular Microbiology. Mol. Micro. 52: 1641-1651.
Wang J. and Chen L. 2003. Domain motions in GroEL upon binding of an oligopeptide. J Mol Biol. 334(3):489-99.
Chen, L. and Sigler, P. 1999. Crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity. Cell, 99:757-768.
Chen, L., Wildegger, G., Kiefhaber, T., Hodgson, K. O., and Doniach, S. 1998. Kinetics of lysozyme refolding: Structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering. J. Mol. Biol. 276:225-237.
