User:Liangcai Gu

Contact Info



 * Liangcai Gu, Ph.D.
 * Dept. of Genetics, Harvard Medical School
 * 77 Ave. Louis Pasteur, NRB 232
 * Boston, MA 02115 USA
 * Email: gulc(at)genetics.med.harvard.edu
 * Lab: (617)432-5917

Dr. Gu currently is a postdoc in George Church lab at Harvard Medical School, and the HHMI Fellow of Jane Coffin Childs Memorial Fund. He is developing a massively parallel technology that bridges transcriptome and proteome studies. It allows functional interrogation and interactome analysis of more than thousands of different protein species in one flow cell.

Education

 * 2003-2008, PhD, University of Michigan, Medicinal Chemistry
 * 1999-2002, MS, Tsinghua University, Biological Chemistry & Molecular Biology
 * 1994-1998, BS, Lanzhou University, Chemistry

Research interests

 * 1) Next-generation DNA sequencing
 * 2) Mechanistic enzymology
 * 3) Interactome, especially for components in biosynthetic/signaling pathways
 * 4) Single-molecule studies
 * 5) Ribosome/translation-based technologies

Research experience
Ph.D. dissertation (University of Michigan): Studies on the biosynthetic pathway of curacin A, a marine cyanobacterial metabolite from Lyngbya majuscula with potent antiproliferative and cytotoxic activities against colon-, renal-, and breast-cancer–derived cell lines.

M.S. thesis (Tsinghua University): Biochemical Studies on the oligomeric structure and molecular chaperone activity of a small hear shock protein, Hsp16.3, an immunodominant antigen which was found to be a major membrane protein of Mycobacterium tuberculosis.

Publications
1.  Gu L, Eisman EB, Dutta S, Franzmann TM, Walter S, Gerwick WH, Skiniotis G, Sherman DH. Tandem acyl carrier proteins in the curacin biosynthetic pathway promote consecutive multienzyme reactions with a synergistic effect. Angew Chem Int Ed Engl. 2011 Mar 14;50(12):2795-8.

2.  Gehret JJ, Gu L, Gerwick WH, Wipf P, Sherman DH, Smith JL. Terminal alkene formation by the thioesterase of curacin a biosynthesis: Structure of a decarboxylating thioesterase. J Biol Chem. 2011 Feb 27. [Epub ahead of print]

3.  Khare D, Wang B, Gu L, Razelun J, Sherman DH, Gerwick WH, Håkansson K, Smith JL. Conformational switch triggered by {alpha}-ketoglutarate in a halogenase of curacin A biosynthesis. Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14099-104.

4.  Gu L, Wang B, Kulkarni A, Gehret JJ, Lloyd KR, Gerwick L, Gerwick WH, Wipf P, Håkansson K, Smith JL, Sherman DH. Polyketide Decarboxylative Chain Termination Preceded by O-Sulfonation in Curacin A Biosynthesis. J Am Chem Soc. 2009 Nov 11;131(44):16033-5.

5.  Gu L, Wang B, Kulkarni A, Geders TW, Grindberg RV, Gerwick L, Håkansson K, Wipf P, Smith JL, Gerwick WH, Sherman DH. Metamorphic enzyme assembly in polyketide diversification. Nature. 2009 Jun 4; 459(7247):731-5.

6.  Jones AC, Gu L, Sorrels CM, Sherman DH, Gerwick WH. New tricks from ancient algae: natural products biosynthesis in marine cyanobacteria. Curr Opin Chem Biol. 2009 Apr; 13(2):216-23.

7.  Sharp K, Arthur KE, Gu L, Ross C, Harrison G, Gunasekera SP, Meickle T, Matthew S, Luesch H, Thacker RW, Sherman DH, Paul VJ. Phylogenetic and chemical diversity of three chemotypes of bloom-forming lyngbya species (Cyanobacteria: Oscillatoriales) from reefs of southeastern Florida. Appl Environ Microbiol. 2009 May; 75(9):2879-88.

8.  Gu L*, Geders TW*, Wang B, Gerwick WH, Håkansson K, Smith JL, Sherman DH. GNAT-like strategy for polyketide chain initiation. Science. 2007 Nov 9; 318(5852):970-4.

9.  Geders TW*, Gu L*, Mowers JC, Liu H, Gerwick WH, Håkansson K, Sherman DH, Smith JL. Crystal structure of the ECH2 catalytic domain of CurF from Lyngbya majuscula. Insights into a decarboxylase involved in polyketide chain beta-branching. J Biol Chem. 2007 Dec 7; 282(49):35954-63.

10. Gu L, Jia J, Liu H, Håkansson K, Gerwick WH, Sherman DH. Metabolic coupling of dehydration and decarboxylation in the curacin A pathway: functional identification of a mechanistically diverse enzyme pair. J Am Chem Soc. 2006 Jul 19; 128(28):9014-5.

11. Fu X, Liu C, Liu Y, Feng X, Gu L, Chen X, Chang Z. Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociation. Biochem Biophys Res Commun. 2003 Oct 17; 310(2):412-20.

12. Abulimiti A, Fu X, Gu L, Feng X, Chang Z. Mycobacterium tuberculosis Hsp16.3 nonamers are assembled and re-assembled via trimer and hexamer intermediates. J Mol Biol. 2003 Feb 28; 326(4):1013-23.

13. Gu L, Abulimiti A, Li W, Chang Z. Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity. J Mol Biol. 2002 May 31; 319(2):517-26.

14. Huang S, Gu L, Mao Q, Chang Z. The effect of Leu122 on the subunit interaction in the reassembly of Hsp16.3 in vitro. Chinese J Biochem Mol Biol, 2002, 18, 99-104 (published in Chinese)