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Protamine-Induced Condensation and Decondensation of the Same DNA Molecule

Brewer, Laurence R., Corzett, Michele, Balhorn, Rod·1999·Science

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, Arg 6 . 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.

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Metadata

Authors
Brewer, L. R., Corzett, M., & Balhorn, R.
Venue
Science
Published
1999-10
Volume
286
Issue
5437
Pages
120-123
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2028029982
Cited by
262
References
0
FWCI
1.63
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Protamine-Induced Condensation and Decondensation of the Same DNA Molecule. https://app.cochat.ai/papers/10.1126/science.286.5437.120
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Brewer, L. R., Corzett, M., & Balhorn, R. (1999). Protamine-Induced Condensation and Decondensation of the Same DNA Molecule. Science. https://doi.org/10.1126/science.286.5437.120

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