Associate Professor CHNG Shu Sin
(Assistant Head - Research & Education)
B.Sc. (Hons), National University of Singapore, 2000-2003; Ph.D., Harvard University, 2004-2010; Postdoctoral fellow, Harvard Medical School, 2010-2011.
Tel: (65)-6516-2682 | Fax: (65)-6779-1691
Recognition and Achievements
- Walter Shaw Young Investigator Award for Lipid Research, the American Society for Biochemistry and Molecular Biology (ASBMB), 2019.
- NUS Annual Teaching Excellence Awards, AY2013/14|AY2014/15.
- Faculty Teaching Excellence Awards, AY2013/14|AY2014/15|AY2015/16; Honour Roll, AY2016/17.
- Christensen Prize for outstanding research achievement, 2009
My group focuses on understanding how biological membranes are assembled in cells using bacterial outer membranes as models. Specifically, we are interested to elucidate the mechanisms of inter-membrane lipid trafficking in Gram-negative bacteria and mycobacteria and to identify protein targets in these bacteria for antibiotics discovery.
[Ref: Shrivastava, R.; et al., Mol. Microbiol. 2017]
Biogenesis of the outer membrane (OM) in Gram-negative bacteria requires the coordinated transport and assembly of proteins and lipids, including lipopolysaccharides (LPS) and phospholipids (PLs), into the membrane. While pathways for LPS and OM protein assembly are well-studied, how PLs are transported to and from the OM is not clear. Mechanisms that ensure OM stability and homeostasis are also unknown. The trans-envelope Tol-Pal complex, whose physiological role has remained elusive, is important for OM stability. Here, we establish that the Tol-Pal complex is required for PL transport and OM lipid homeostasis in Escherichia coli. Cells lacking the complex exhibit defects in lipid asymmetry and accumulate excess phospholipids (PLs) in the OM. This imbalance in OM lipids is due to defective retrograde PL transport in the absence of a functional Tol-Pal complex. Thus, cells ensure the assembly of a stable OM by maintaining an excess flux of PLs to the OM only to return the surplus to the inner membrane.
- CM3225 Biomolecules
- CM4227 Chemical Biology
- Ercan, B.; Low, W.-Y.; Liu, X.; Chng, S.-S., Characterization of interactions and phospholipid transfer between substrate binding proteins of the OmpC-Mla system. Biochemistry 2018, in press. (invited contribution as part of "Future of Biochemistry: The International Issue" (Jan 2019)).
- Yeow, J.; Tan, K. W.; Holdbrook, D. A.; Chong, Z. S.; Marzinek, J. K.; Bond, P. J.; Chng, S.-S., The architecture of the OmpC-MlaA complex sheds light on the maintenance of outer membrane lipid asymmetry in Escherichia coli. J. Biol. Chem. 2018, 293(29), 11325-11340.
- Shrivastava, R.; Jiang, X. E.; Chng, S.-S., Bacterial outer membrane homeostasis via retrograde phospholipid transport in Escherichia coli. Mol. Microbiol. 2017, 106(3), 395-408.
- Xu, Z. J.; Meshcheryakov, V. A.; Poce, G.; Chng, S.-S., MmpL3 is the flippase for mycolic acids in mycobacteria.Proc. Natl. Acad. Sci. U.S.A. 2017, 114(30), 7993-7998.
- Thong, S. H.; Ercan, B.; Torta, F.; Fong, Z. Y.; Wong, H. Y.; Wenk, M.R.; Chng, S.-S., Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry. eLife 2016, 5 , e19042.
- Chong, Z.-S.; Woo, W.-F.; Chng, S.-S., Osmoporin OmpC forms a complex with MlaA to maintain outer membrane lipid asymmetry in Escherichia coli. Mol. Microbiol. 2015, 98, 1133-1146.