Zeng-Yi CHANG Personal Data: Zengyi Chang Current Positions Associate Dean Director Editorial Board Journal of Biological Chemistry Protein Science

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1 Zeng-Yi CHANG Personal Data: Name: Zengyi Chang Birthday: January 5, 1965 Citizenship: People s Republic of China Contacting Information: School of Life Sciences, Peking University, Beijing, P. R. China, Tel: Fax: ; Personal introductin website: Lab website: Current Positions: Associate Dean, College of Life Sciences, Peking University; Director, Center for Protein Science, Peking University (starting July 1, 2008); Editorial Board Editorial Board member, Journal of Biological Chemistry (starting July 1, 2008) Editorial Advisory Board member, Protein Science (a publication of the Protein Society); Editorial Board member, IUBMB Life (a publication of International Union of Biochemistry and Molecular Biology); Executive Vice Editor-in-Chief Science in China Series C: Life Sciences (Starting June, 2008) Editorial Board Member, Biochemistry and Molecular Biology Education (a publication of IUBMB); Vice Editor-in-Chief, Chinese Journal of Biochemistry and Molecular Biology Editor, Acta Biochimica et Biophysica Sinica. Guest editor, IUBMB Life Special Issue in celebration of the 21 st IUBMB and 12 th FAOBMB International Congress of Biochemistry and Molecular Biology to be held in Shanghai, China, August 2-7, Professional Organization Executive Council Member, The Protein Society Member, the Chinese Committee for the International Council for Science (ICSU-China); Executive Council Member, Chinese Association of Biochemistry and Molecular Biology. Vice President, Secretary-general, President-Elect, Chinese Protein Society. Member, Advisory Committee for University Education in Biological Sciences, Ministry of Education, People s Republic of China.

2 Member, Expert Committee for the Protein Study Plan ( ), Ministry of Science and Technology, People s Republic of China. Education: 1984 B.S., Biology, East China Normal University, Shanghai, China Graduate Student, Shanghai Institute of Biochemistry, Chinese Academy of Sciences, Shanghai, China , English Training, Guangzhou English Learning Center (GELC), Sun Yat-Sen University, Guangzhou, China Ph.D., Biochemistry, Baylor College of Medicine, Houston, Texas, USA. Ph.D. Thesis: Probing the Roles of the Highly Conserved Amino Acids in the Catalytic Activity of Adenosine Deaminase, Advisor: Dr. Rodney, E. Kellems (currently the Chairman of the Department of Biochemistry and Molecular Biology, University of Texas-Houston Medical School). Postdoctoral Training: Research Associate, Howard Hughes Medical Institute, Baylor College of Medicine (in Dr. Florante A. Quiocho s lab). Academic Appointments: Associate Professor, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, P. R. China /2003 Professor, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, P. R. China. Jun.-Sept., 2002 Visiting Professor, Harvard Medical School, Boston, USA. 9/2003-Present Professor, Department of Biochemistry and Molecular Biology, College of Life Sciences, Peking University, Beijing, P. R. China Honors and Awards: 1985 The CUSBEA (The China-United States Biochemistry and Molecular Biology Examination and Application) Fellowship Robert A. Welch Foundation Predoctoral Fellowship Excellent Publication Award, Tsinghua University National Outstanding Young Scientist Award, P. R. China. Oral Presentations at International Conferences: 1. Protein Structure, Stability, and Folding: Fundamental and Medical Aspects, June 22-26, 1998, Moscow, Russia (invited speaker) nd International Workshop on Molecular Biology of Stress Response, October 15-18, 1999, Wuhan, China th FAOBMB (Federation of Asian & Oceanian Biochemists and Molecular Biologists) Symposium, October 21-24, 2000, Beijing, China. (Plenary speaker) 4. Recent Progress in Biotechnology, March 27-28, 2000, Singapore.

3 5. Leading Biotechnology toward the Twenty-first Century, April 7-8, 2000, Vancouver, Canada. 6. World Conference on Science and Technology, September 13-15, 2001, Manila, the Philippines. (Plenary speaker) 7. The 10 th Congress of FAOBMB (Federation of Asian & Oceanian Biochemists and Molecular Biologists), December 7-11, 2003, Bangalore, India (invited speaker) th International Workshop on the Molecular Biology of Stress Response; May 13-16, 2004; Wuhan and Yichang, China. (Honorable speaker) 9. 20th IUBMB International Congress of Biochemistry and Molecular Biology and 11 th FAOBMB Congress, June 17-13, 2006, Kyoto, Japan (Invited speaker) th Symposium of the Protein Society, Aug. 4-9, 2006, San Diego, USA th IUBMB Conference, May 21-27, 2007, Salvador, Brazil (invited speaker). 12. The 2 nd Pacific Rim International Conference on Protein Science, June 22-27, 2008, Cairns, Australia. 13. The second China-Australia Biomedical Research Conference, April 24-27, 2009, Tianjin, China (invited speaker). 14. The 23 rd Protein Society Symposium, July 24-29, 2009, Boston, USA (invited speaker). 15. The 21 st IUBMB International Congress of Biochemistry and Molecular Biology, Aug. 2-7, 2009, Shanghai, China (invited speaker). Current Research Interests: 1. The biology of protein homo-oligomerization; 2. Immediate response of stress proteins towards stress conditions; 3. Action mechanisms of molecular chaperones; 5. Protein stability and foldability; 6. Protein-protein interactions in living cells. 7. Molecular Mechanism of Aging and Dormancy. Selected Publications:( corresponding author papers indicated by *) *55. Chang Z (2009) Posttranslational Modulation of the Biological Activities of Molecular Chaperones, Sci. China Ser.C Life Sci., 52(6): *54. Chang, Z. (2009) The CUSBEA Program: Twenty Years Later, IUBMB Life, 61(6): *53. Wang,Y. Ezemaduka, A. N., Tang, Y. and Chang, Z., (2009) Understanding the Mechanism of the Dormant Dauer Formation of C. elegans: From Genetics to Biochemistry, IUBMB Life,61(6): (Invited critical review) *52. Jiang J, Zhang X, Chen Y, Wu Y, Zhou ZH, Chang Z, Sui SF.(2008) Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins Proc Natl Acad Sci U S A, 105(33): *51. Wu, Y., Hong, W., Zhang, L., and Chang, Z. (2008) Conserved Amphiphilic Feature Is Essential for Periplasmic Chaperone HdeA to Support Acid Resistance in Enteric Bacteria, Biochem. J.,412: *50. Liu, C., Mao, K., Zhang, M., Sun, Z., Hong, W., Li, C., Peng, B., and Chang, Z. (2008) The SH3-Like Domain Switches Its Interaction Partners to Modulate the Repression Activity of Mycobacterial Iron-Dependent Transcription Regulator

4 (IdeR) in Response to Metal Ion Fluctuations, J. Biol. Chem., 283(4): *49. Jiao, W., Hong, W., Li, P., Sun, S., Ma, J., Qian, M., Hu, M., and Chang, Z. (2008) The Dramatically Increased Chaperone Activity of Small Heat Shock Protein IbpB is Retained for an Extended Period of Time after the Stress Condition is Removed, Biochem. J., 410(1):63-70 *48. Ma, J., Ge, X., and Chang, Z. (2007) Protein function studies: history, current status and future trends, Chinese Bull. Life Sci. 19(3): (Invited Review, in Chinese) *47. Qin, Y., Wang, H., and Chang, Z. (2007) HSP12.1, A small heat shock protein in C. elegans, has chaperone-like activity, Prog. Biochem. Biophys. 34(6): (In Chinese) *46. Feng, Y., Jiao, W., Fu, X., and Chang, Z. (2006) Stepwise disassembly and apparent non-stepwise reassembly for the oligomeric RbsD protein, Protein Science., 15(6): *45. Fu, X., and Chang, Z. (2006) Identification of bis-ans binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism Biochem. Biophys. Res. Commun, 349: *44. Fu, X. and Chang, Z. (2006) Phylogenetic and biochemical studies reveal a potential evolutionary origin of animal small heat shock proteins from bacterial class A J. Mol. Evol., 62: Fedurkina, N.V., Belousova, L.V., Mitskevich, L.G., Zhou, H.-M., Chang, Z., and Kurganov, B.I. (2006) The change in the kinetic regime of protein aggregation with temperature increase: Thermal aggregation of rabbit muscle creatine kinase, Biochemistry-Moscow, 71(3): *42. Zhang, X., Zheng, Y., and Chang, Z. (2006) Peptide Induced Conformational Changes of E. coli DegP (HtrA) Protease, Prog. Biochem. Biophy., 33(2): (In Chinese) *41. Fu, X. and Chang, Z (2006) Identification of a highly conserved Pro-Gly in non-animal small heat shock proteins and characterization of its structural and functional roles in Mycobacterium tuberculosis Hsp16.3 Biochemistry-Moscow, 69(5): *40. Jiao, W., Li, P., Zhang, J., Zhang, H., Chang, Z. (2005) Small Heat Shock Proteins Function in the Insoluble Protein Complex, Biochem Biophys Res Commun, 335(1): *39. Hong, W., Jiao, W., Hu, J., Zhang, J., Liu, C., Fu, X., Shen, D., Xia, B., and Chang, Z. (2005) Periplasmic Protein HdeA Exhibits Chaperone-like Activity Exclusively within Stomach ph Range by Transforming into Disordered Conformation, J. Biol. Chem., 280(29): *38. Chen, X., Fu, X., Ma, Y., and Chang, Z. (2005) Chaperone-like activity of Mycobacterium tuberculosis Hsp16.3 does not require its intact (native) structures, Biochemistry-Moscow, 70(8): *37. Fu, X., Zhang, H., Zhang, X., Cao, Y., Jiao, W., Liu, C., Song, Y., Abulimiti, A., and Chang, Z. (2005) A dual role for the N-terminal region of Mycobacterium

5 tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins J. Biol. Chem., 280 (8) : *36. Zhang, H. Fu, X. Jiao, W., Zhang, X., Liu, C., and Chang, Z. (2005) The association of small heat shock protein Hsp16.3 with the plasma membrane of Mycobacterium tuberculosis: dissociation of oligomers is a prerequisite Biochem Biophys Res Commun, 330: *35. Jiao W., Qian, M., Li, P., Zhao, L., and Chang, Z. (2005) The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli J. Mol. Biol., 347(4): *34. Fu, X., Zhang, X., and Chang, Z. (2005) 4'-dianilino-1,1'-binaphthyl-5,5'-sulfonate (bis-ans), a novel molecule having chaperone-like activity, Biochem Biophys Res Commun, 329: *33. Zhang, X., Fu, X., Zhang, H., Liu, C. Jiao, W., and Chang, Z. (2005) Chaperone-like Activity of -Casein, Interna. J. Biochem.Cell Biol., 37: *32. Liu, C. He., Y. and Chang Z. (2004) Truncated hemoglobin of Mycobacterium tuberculosis: The oligomeric state change and the interaction with membrane components Biochem Biophys Res Commun. 316: *31. Liu Y., Fu, X., Shen, J., Zhang, H., Hong, W., and Chang, Z. (2004) Periplasmic proteins of Escherichia coli are highly resistant to aggregation: A reappraisal for roles of molecular chaperones in periplasm Biochem Biophys Res Commun. 316(3): *30. Fu, X. and Chang, Z. (2004) Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis Biochem Biophys Res Commun. 316: *29. Zhang, X. and Chang Z. (2004) Temperature-dependent protease activity and structural properties of human HtrA2 protease Biochemistry-Moscow, 69(6): *28. Fu, X., Jiao, W., Abulimiti, A. and Chang, Z. (2004) Inter-subunit cross-linking suppressed the dynamic oligomeric dissociation of Mycobacterium tuberculosis Hsp16.3 and reduced its chaperone activity Biochemistry-Moscow, 69(5): Chang, Z. and Jiao, W. (2004) Discovering a cellular pathway on energy-consuming protein degradation The story behind the Nobel Prize in Chemistry 2004, Acta Biophysica Sinia, 20(6): (Invited review, in Chinese) *26. Fu X, Li W, Mao Q, Chang Z. (2003) Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: implications for the evolution of cysteine in molecular chaperones Biochem Biophys Res Commun. 308(3): *25. Fu, X. Liu, C., Liu, Y., Feng, X., Gu, L., Chen, X., and Chang, Z Small Heat Shock Protein Hsp16.3 Modulates Its Chaperone Activity by Adjusting the Rate of Oligomeric Dissociation. Biochem Biophys Res Commun.

6 310(2): *24. Abulimiti, A., Fu, X., Gu., L., Feng, X., and Chang, Z. (2003) " Mycobacterium tuberculosis Hsp16.3 Nonamers are Assembled and Re-assembled via Trimer and Hexamer Intermediates " J. Mol. Biol. 326(4): *23. Abulimiti, A., Qiu, X., Chen, J., Liu, Y., and Chang, Z. (2003) Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants Biochem. Biophys. Res. Commun., 305(1): *22. Abulimiti, A. and Chang, Z. (2003) "Alpha-crystallin promotes the assembly of trimeric form of the Mycobacterium tuberculosis Hsp16.3 in cell free system" Biochemistry (Moscow), Chen Y, Lu YJ, Wang HW, Quan S, Chang Z, Sui SF. (2003) Two-dimensional crystallization of a small heat shock protein HSP16.3 on lipid layer Biochem Biophys Res Commun. 310(2): *20. Gu, L., Abulimiti, A., Li, W., and Chang, Z. (2002) "Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisit for chaperone-like activity" J. Mol. Biol *19. Feng, X., Huang, S. Fu, X., Abulimiti, A. and Chang, Z. (2002) "The reassembling process of the nonameric Mycobacterium tuberculosis small heat shock protein Hsp16.3 occurs via a stepwise mechanism" Biochem. J., 363: Xiu, Z., Chang, Z., Zeng, A. (2002) "Nonlinear Dynamics of Regulations of Bacterial trp operon: Model Analysis of Integrated Effects of Repression, Feedback Inhibition, and Attenuation" Biochnol. Prog. 18: Pan, G. J., Chang, Z.Y., Scholer, H.R., and Pei, D. Q. (2002) Stem cell pluripotency and transcription factor Oct4 Cell Research 12(5-6): *16. Mao, Q., Ke, D., Feng, X. and Chang, Z. (2001) Preheat Treatment for Mycobacterium tuberculosis Hsp16.3: Correlation Between a Structural Phase Change at 60 o C and a Dramatic Increase in Chaperone-like Activity Biochem. Biophys. Res. Commun., 284: *15. Mao, Q., Chang, Z. (2001) Site-directed Mutation on the only Universally Conserved Residue Leu122 of Small Heat Shock Protein Hsp16.3 Biochem. Biophys. Res. Commun., 289(5): *14. Mao, Q., Ke, D., Chang, Z. (2001) Electrostatic interaction plays an essential role for Mycotacterium tuberculosis Hsp16.3 to interact with substrate proteins Biochemistry (Moscow), 66(8): *13. Mao, Q., Ke, D., and Chang, Z. (2001) "Heat treatment of small heat shock proteins alpha-crystallin and Hsp16.3: Structure changes vs. Chaperone like activity" Tsinghua Sci. Technol., 6(5): Chen, Y., An, J., Ding, Y., Dai, H., Mao, Q., Feng, L., Liu, B., Chang, Y., Chen, F., He, H., Tang, H., Chang, Z., and Rao, ZH (2001) Preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis Hsp16.3 molecular chaperone Protein and Peptide letters, 8(6):

7 *11. Dai, H., Mao, Q., Yang, H., and Chang, Z. (2000) Probing the Roles of the Only Universally Conserved Leucine Residue in the Oligomerization and Chaperone-like Activity of Mycobacterium tuberculosis Small Heat Shock Protein Hsp16.3, J. Protein Chem., 19(4): Wang, L., Duan, M., Zhang, Y. Lin S., and Chang, Z. (2000) Translocation of P53-regulated laminin receptors in pro-apoptotic microcircustance of human vasculogenesis inhibition, Cell Biol. Interna., 24(10): Xiu, Z., Chang, Z., and Su. Z. (2000) Review of Biotechnology in the 20 th Century and perspectives in the 21 st century, J. Nature, 22(4): (In Chinese) *8. Yang, H., Huang, S., Dai, H., Gong, Y., Zheng, C., and Chang, Z. (1999), The Mycobacterium tuberculosis small heat shock protein HSP16.3 Exposes Hydrophobic Surfaces at Mild Conditions: Conformational Flexibility and Molecular Chaperone Activity, Protein Science, 8(1): Chang, Z., Wilson, D.K., Kellems, R.E., and Quiocho, F.A. (1997) Cysteine not Required for the Catalytic Activity of Adenosine Deaminase Tsinghua Sci. Technol. (published in English), 2(1): Chang, Z., Primm, T.P., Jakana, J., Lee, I.H., Chiu, W., Gilb ert, H.F., and Quiocho, F.A. (1996) Mycobacterium tuberculosis 16-kDa Antigen (HSP16.3) Functions as an Oligomeric Structure in Vitro to Suppress Thermal Aggregation J. Biol. Chem., 271(12): Sideraki, V., Mohamedali, K.A.,Wilson, D.K., Chang, Z., Kellems, R.E., Quiocho, F.A., and Rudolph, F.B. (1996) Probing the Functional Role of Two Conserved Active Site Aspartates in Mouse Adenosine Deaminase Biochemistry, 35(4): Chang, Z., Choudhary, A. Lathigra, R. and Quiocho, F.A. (1994) The Immunodominant 38-kDa Lipoprotein Antigen of Mycobacterium tuberculosis Is a Phosphate-binding Protein J. Biol. Chem., 269(3): Chouhary, A., Vyas, M. N. Vyas, N. K. Chang, Z. and Quiocho, F.A. (1994) Crystallization and Preliminary X-ray Crystallographic Analysis of the 38-kDa Immunodominant Antigen of Mycobacterium tuberculosis Protein Science, 3(12): Sharff, A. J., Wilson, D. K., Chang, Z. and Quiocho, F. A. (1992) Refined 2.5 A Structure of Murine Adenosine Deaminase at ph 6.0 J. Mol. Biol., 226(4): Chang, Z., Nygaard, P., Chinault, A. C., and Kellems, R. (1991) Deduced Amino Acid Sequence of Escherichia coli Adenosine Deaminase Reveals Evolutionarily Conserved Amino Acid Residues: Implications for Catalytic Function Biochemistry, 30(8):

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