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J. Biol. Chem., Vol. 278, Issue 43, 42403-42408, October 24, 2003

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Dynamics of Protamine 1 Binding to Single DNA Molecules^*

Laurence Brewer, Michele Corzett¶, Edmond Y. Lau¶, and Rod Balhorn¶||

From the Electronic Engineering Technologies Division and ^¶Biology and Biotechnology Research Program, Lawrence Livermore National Laboratory, Livermore, California 94550

Protamine molecules bind to and condense DNA in the sperm of most vertebrates, packaging the sperm genome in an inactive state until it can be reactivated following fertilization. By using methods that enable the analysis of protamine binding to individual DNA molecules, we have monitored the kinetics of DNA condensation and decondensation by protamine 1 (P1) and synthetic peptides corresponding to specific segments of the bull P1 DNA binding domain. Our results show that the number of clustered arginine residues present in the DNA binding domain is the most important factor affecting the condensation and stability of the DNA-protamine complex prior to the formation of inter-protamine disulfide cross-links. The high affinity of P1 for DNA is achieved by the coordinated binding of three anchoring domains, which together in bull P1 contain 19 Arg residues. The single DNA molecule experiments show that sequences containing two or more anchoring domains have an off-rate that is at least 3 orders of magnitude slower than those containing a single domain. The use of Arg, rather than Lys residues, and the inclusion of Tyr or Phe residues in the hinge regions between anchoring domains provide additional stability to the complex.

Received for publication, April 7, 2003 , and in revised form, August 8, 2003.

^* This work was supported in part by the United States Department of Energy by the University of California, Lawrence Livermore National Laboratory, under Contract W-7405-Eng-48. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by NICHD Grant 1 K25 HD01387-03 from the National Institutes of Health.

^|| To whom correspondence should be addressed. Tel.: 925-422-6284; Fax: 925-422-2282; E-mail: balhorn2{at}llnl.gov.

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