Feng Gong

Assistant Professor of Biochemistry
and Molecular Biology

Ph.D.  (1998) The Chinese Academy of Sciences, China.

Nucleotide Excision Repair, Chromatin Remodeling, Cell Cycle Regulation

Tel: (305) 243-9270, Fax: (305) 243-3955

fgong@med.miami.edu

 Research Interests: 

We are interested in understanding the molecular basis of chromatin dynamics during nucleotide excision repair (NER). Maintenance of genomic integrity is of fundamental importance to all living organisms. Defects in DNA repair are found in human diseases associated with increased cancer frequency.

In eukaryotic cells, DNA is packaged with histones and other accessory proteins into chromatin. Thus DNA repair enzymes must deal with the highly compact and dynamic structure of chromatin. Indeed, significant structural rearrangements at the nucleosome level of chromatin during NER were uncovered more than two decades ago. However, we know surprisingly little about how NER is operated in the chromatin environment. Recently, others and we have found evidence that the Swi/Snf chromatin remodeling complex plays an important role during NER.

Swi/Snf complexes are ubiquitously expressed, prototypical “ATP-dependent chromatin remodeling complexes” that can use energy to manipulate nucleosome structure in response to various signals. We found that UV damage can stimulate Swi/Snf’s association with NER proteins involved in DNA damage recognition. But it is not understood how Swi/Snf functions during NER. We are applying biochemical and genetic approaches to define the role of Swi/Snf in NER in the yeast Saccharomyces cerevisiae.

In mammalian cells, several subunits of the human Swi/Snf complex are tumor suppressors that control cell cycle transitions. Recently, we have found that the human Swi/Snf complex plays a role in the cellular response to UV damage via regulation of Gadd45a and p21 expression. Using a combination of genetic and molecular biological approaches, we are characterizing novel genes that are regulated by Swi/Snf in human cells. 

Our laboratory employs mammalian cell culture and budding yeast as model systems to address basic questions concerning the regulation/or modifications of chromatin in response to DNA damage. Studying the role of chromatin remodeling complexes in DNA damage response will improve our understanding of the mechanisms of genome instability and carcinogenesis.

Representative Publications: 

1. R. Nag, F. Gong, D. Fahy and M. Smerdon. 2008. A single amino acid change in histone H4 enhances UV survival and DNA repair in yeast. Nucleic Acids Res. In press 

2. F. Gong, D. Fahy, H. Liu, W. Wang and M. Smerdon. 2008. Role of the mammalian SWI/SNF chromatin remodeling complex in the cellular response to UV damage. Cell Cycle 7(8): 1069-1076 [FG is a corresponding author]

3. F. Gong, D. Fahy and M. Smerdon. 2006. Rad4–Rad23 interaction with SWI/SNF links ATP-dependent chromatin remodeling with nucleotide excision repair. Nature Structural & Molecular Biology 13: 902 – 907.  [FG is a corresponding author]

4. F. Gong, Y Kwon and M.J. Smerdon. 2005. Nucleotide excision repair in chromatin and the right of entry. DNA Repair 4(8): 884-96.

5. F. Gong and C. Yanofsky. 2003. A transcriptional pause synchronizes translation with transcription in the tryptophanase operon leader region. J Bacteriol. 185(21): 6472-6.

6. F. Gong and C. Yanofsky. 2002. Instruction of translating ribosome by nascent peptide. Science, 297: 1864-7.

7. F. Gong and C. Yanofsky. 2002. Analysis of tryptophanase operon expression in vitro: accumulation of TnaC-peptidyl-tRNA in S-30 extracts depleted of release factor 2 prevents Rho-factor action, simulating induction. J. Biol. Chem, 277(19): 17095-100.

8. F. Gong, K. Ito, Y. Nakamura and C. Yanofsky. 2001. The mechanism of tryptophan induction of tryptophanase operon expression: tryptophan inhibits release factor 2 mediated cleavage of TnaC-peptidyl-tRNA^Pro. Proc. Natl. Acad. Sci. USA, 98(16): 8997-9001.

9. F. Gong and C. Yanofsky. 2001. Reproducing tna operon regulation in vitro in an S-30 system: tryptophan induction inhibits cleavage of TnaC-tRNA. J. Biol. Chem. 276(3): 1974-83.

Honors and Professional Activities

Postdoctoral Research: Stanford University

Research Assistant Professor: Washington State University