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Vol. 96, Issue 15, 8557-8561, July 20, 1999

Biochemistry / Genetics
 Gene silencing via protein-mediated subcellular localization of DNA

(membrane patches of DNA-binding proteins / chromatin sequestration / gene repression in Escherichia coli / position effects in eukaryotes / SopB protein)

Sook-Kyung Kim and James C. Wang*

Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138

Contributed by James C. Wang, May 4, 1999

We previously reported that overexpression of SopB, an Escherichia coli F plasmid-encoded partition protein, led to silencing of genes linked to, but well-separated from, a cluster of SopB-binding sites termed sopC. We show here that in this SopB-mediated repression of sopC-linked genes, all but the N-terminal 82 amino acids of SopB can be replaced by the DNA-binding domain of a sequence-specific DNA-binding protein, provided that the sopC locus is also replaced by the recognition sequence of the DNA-binding domain. These results, together with our previous finding that the N-terminal fragment of SopB is responsible for its polar localization in cells, suggest a mechanism of gene silencing: patches of closely packed DNA-binding domains are formed if a sequence-specific DNA-binding protein is localized to specific cellular sites; such a patch can capture a DNA carrying the recognition site of the DNA-binding domain and sequestrate genes adjacent to the recognition site through nonspecific binding of DNA. The generalization of this model to gene silencing in eukaryotes is discussed.

*   To whom reprint requests should be addressed. e-mail: jcwang{at}fas.harvard.edu.

Copyright © 1999 by The National Academy of Sciences  0027-8424/99/968557-5$2.00/0
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Related Commentary in PNAS:

On the mechanism of silencing in Escherichia coli
Jasper Rine
PNAS 1999 96: 8309-8311. [Extract] [Full Text]  



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