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Jong-Hee Lee, Ph.D.
My research field is characterization of gene regulation and expression in M. tuberculosis. Gene expression is initiated by RNA polymerase binding to the promoter of target genes. Bacterial RNA polymerase is composed of a core enzyme and one of several different sigma factors. The sigma factor determines promoter specificity by recognizing and binding to the -10 sequence of the promoter. Thus, the investigation of sigma factor expression in Mycobacterium tuberculosis is important for understanding gene expression during infection. The adaptation of pathogenic bacteria to different environments is an essential feature of survival and pathogenicity. Bacteria are exposed to stresses such as nutrient limitation and antimicrobial products of the immune system during infection of the host. Mycobacteria can survive in macrophages, which represent a stringent and nutrient-deficient environment. To understand the changes in patterns of gene expression in response to environmental signals (nutrition, temperature, pH) in M. tuberculosis, the gene expression of sigma factors must be thoroughly investigated.
To read some of these publications online, click here. Please note that to read the full text of some of these articles requires that you have an online subscription to the journal.
1. Lee, J.H., P. C. Karakousis, and W. R. Bishai. 2008. Roles of SigB and SigF in the Mycobacterium tuberculosis sigma factor network. J Bacteriol 190:699-707.
2. Lee, J.H., D. E. Geiman, and W. R. Bishai. 2008. Role of stress response sigma factor SigG in Mycobacterium tuberculosis. J Bacteriol 190:1128-33.
3. Williams, E. P., J.H. Lee, W. R. Bishai, C. Colantuoni, and P. C. Karakousis. 2007. Mycobacterium tuberculosis SigF regulates genes encoding cell wall-associated proteins and directly regulates the transcriptional regulatory gene phoY1. J Bacteriol 189:4234-42.
4. Lee, J.H., S. H. Ahn, E. M. Lee, S. H. Jeong, Y. O. Kim, S. J. Lee, and I. S. Kong. 2005. The FAXWXXT motif in the carboxyl terminus of Vibrio mimicus metalloprotease is involved in binding to collagen. FEBS Lett 579:2507-13.
5. Ahn, S. H., J. H. Han, J.H. Lee, K. J. Park, and I. S. Kong. 2005. Identification of an iron-regulated hemin-binding outer membrane protein, HupO, in Vibrio fluvialis: effects on hemolytic activity and the oxidative stress response. Infect Immun 73:722-9.
6. Lee, E. M., S. H. Ahn, J. H. Park, J.H. Lee, S. C. Ahn, and I. S. Kong. 2004. Identification of oligopeptide permease (opp) gene cluster in Vibrio fluvialis and characterization of biofilm production by oppA knockout mutation. FEMS Microbiol Lett 240:21-30.
7. Lee, J.H., S. H. Ahn, E. M. Lee, Y. O. Kim, S. J. Lee, and I. S. Kong. 2003. Characterization of the enzyme activity of an extracellular metalloprotease (VMC) from Vibrio mimicus and its C-terminal deletions. FEMS Microbiol Lett 223:293-300.
8. Kim, S. H., S. H. Ahn, J.H. Lee, E. M. Lee, N. H. Kim, K. J. Park, and I. S. Kong. 2003. Genetic analysis of phosphomannomutase/phosphoglucomutase from Vibrio furnissii and characterization of its role in virulence. Arch Microbiol 180:240-50.
9. Lee, J.H., S. H. Ahn, S. H. Kim, Y. H. Choi, K. J. Park, and I. S. Kong. 2002. Characterization of Vibrio mimicus phospholipase A (PhlA) and cytotoxicity on fish cell. Biochem Biophys Res Commun 298:269-76.
10. Han, J. H., J.H. Lee, Y. H. Choi, J. H. Park, T. J. Choi, and I. S. Kong. 2002. Purification, characterization and molecular cloning of Vibrio fluvialis hemolysin. Biochim Biophys Acta 1599:106-14.
11. Lee, S. J., J.H. Lee, H. J. Jin, H. Y. Ryu, Y. Kim, I. S. Kong, and K. W. Kim. 2000. A novel technique for the effective production of short peptide analogs from concatameric short peptide multimers. Mol Cells 10:236-40.
12. Lee, J.H., G. T. Kim, J. Y. Lee, H. K. Jun, J. H. Yu, and I. S. Kong. 1998. Isolation and sequence analysis of metalloprotease gene from Vibrio mimicus. Biochim Biophys Acta 1384:1-6.
13. Kang, J. H., J.H. Lee, J. H. Park, S. H. Huh, and I. S. Kong. 1998. Cloning and identification of a phospholipase gene from Vibrio mimicus. Biochim Biophys Acta 1394:85-9.
The method of overexpression of the promoter region of alginate lyase gene from marine bacteria, Pseudomonas sp., in E.coli : Korea patent No.10-1999-0021956