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Protamine-induced condensation and decondensation of the same DNA molecule

Brewer, L.R., Corzett, M., and Balhorn, R. (1999) Protamine-induced condensation and decondensation of the same DNA molecule. Science, 286 (5437). pp. 120-123. ISSN 0036-8075 (doi:10.1126/science.286.5437.120)

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Publisher's URL: http://dx.doi.org/10.1126/science.286.5437.120

Abstract

The DNA in sperm and certain viruses is condensed by arginine-rich proteins into toroidal subunits, a form of packaging that inactivates their entire genome. Individual DNA molecules were manipulated with an optical trap to examine the kinetics of torus formation induced by the binding of protamine and a subset of its DNA binding domain, Arg6. Condensation and decondensation experiments with λ-phage DNA show that toroid formation and stability are influenced by the number of arginine-rich anchoring domains in protamine. The results explain why protamines contain so much arginine and suggest that these proteins must be actively removed from sperm chromatin after fertilization.

Item Type:Article
Status:Published
Refereed:Yes
Glasgow Author(s):Brewer, Dr Laurence
Authors: Brewer, L.R., Corzett, M., and Balhorn, R.
College/School:College of Science and Engineering > School of Physics and Astronomy
Journal Name:Science
Publisher:American Association for the Advancement of Science
ISSN:0036-8075
ISSN (Online):1095-9203

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