How to Part Ways

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Science  12 Oct 2012:
Vol. 338, Issue 6104, pp. 172
DOI: 10.1126/science.338.6104.172-b

Proteins perform critical functions in the cell, serving as structural units, enzymes, and transcription factors, among other roles. Protein activity can be static, as for some structural proteins, or dynamic, as in the case of transcription factor binding to gene promotors. In many cases, once transcription begins, transcription factor binding is no longer needed and in fact needs to be terminated so that other regulatory factors can act at that site. How this occurs, however, is not well understood. Zelin et al. now provide one such example. They show that the molecular chaperone p23 functions to disassemble protein-DNA complexes that include heat shock factor 1 or the DNA replication factor CDC6. Subsequently, covalent modification via acetylation of lysine residues by GCN1 can extend this dissociated state. Such dynamic interplay among a multitude of factors provides insight into how complex DNA regulation is mediated.

Mol. Cell 47, 10.1016/j.molcel.2012.08.026 (2012).

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