Michael Bustin, Ph.D.
Dr. Bustin studies the role of chromosomal proteins in chromatin function, epigenetic regulation, development and disease, including cancer.
Chromosomal Proteins and Chromatin Function
Precise and specific interactions between chromosomal proteins and the chromatin fiber play a key role in epigenetic regulation, transcription, replication and DNA repair and therefore affect the orderly progression of biological processes such as development and differentiation. Numerous diseases, including cancer, are associated with changes in chromatin structure and function. The research aim of the Protein Section is to study the molecular mechanisms whereby nuclear proteins affect the structure and function of chromatin and play a role in establishing the cellular phenotype. The focus is on architectural proteins such as HMGN, the linker histone H1 and additional members of the high mobility group (HMG) protein family, which have been shown to affect the structure and function of chromatin and play a role in development and disease.
The laboratory employs a multidisciplinary approach, including analysis of transgenic and knock-out mice, and methodologies used in molecular biology, biochemistry, cell biology and immunochemistry, to study:
1. Molecular mechanisms whereby chromosomal proteins modulate gene expression from chromatin.
2. Mechanisms whereby HMGN chromosomal proteins affect the cellular phenotype and modulate embryonic differentiation.
3. The role of HMGN chromosomal proteins in modulating DNA repair processes.
4. The role of architectural chromatin binding proteins in epigenetic regulation.
5. Global organization of architectural proteins in the nucleus and in chromatin and their role in chromatin dynamics.
For more details about our research program, list of publications, and representative results please visit the Bustin Laboratory Web site.
Selected Key Publications
- Nature Communication. 2018. [ Journal Article ]
- Science. 352(6286): aad6933, 2016. [ Journal Article ]
Functional compensation among HMGN variants modulates the DNase I hypersensitive sites at enhancers.Genome Res. 25(9): 1295-308, 2015. [ Journal Article ]
The interaction of NSBP1/HMGN5 with nucleosomes in euchromatin counteracts linker histone-mediated chromatin compaction and modulates transcription.Mol. Cell. 35: 642-56, 2009. [ Journal Article ]
- Nat. Struct. Mol. Biol. 13: 305-10, 2006. [ Journal Article ]
Michael Bustin received his Ph.D. from University at California, Berkeley and did postdoctoral work in the area of protein chemistry, in the laboratory of Drs. S. Moore and W. Stein at the Rockefeller University in New York, and in the area of immunochemistry at the Weizmann Institute of Science, Israel, where he produced antibodies to histones and pioneered their use for studies on chromatin structure and function. His research interests center on the role of chromosomal proteins in chromatin function, gene expression, development and cancer.
|Takashi Furusawa Ph.D.||Staff Scientist|
|Bing He Ph.D.||Postdoctoral Fellow (Visiting)|
|Ravikanth Nanduri Ph.D.||Postdoctoral Fellow (Visiting)|
|Yuri V. Postnikov M.D., Ph.D.||Staff Scientist|
|Shaofei Zhang Ph.D.||Research Fellow|