Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1996 Jul 5;271(27):16350-6.

Interaction of human immunodeficiency virus nucleocapsid protein with a structure mimicking a replication intermediate. Effects on stability, reverse transcriptase binding, and strand transfer

J J DeStefano  1
Affiliations
  • PMID: 8663119
Free article

Interaction of human immunodeficiency virus nucleocapsid protein with a structure mimicking a replication intermediate. Effects on stability, reverse transcriptase binding, and strand transfer

J J DeStefano. J Biol Chem. .
Free article

Abstract

The interaction of human immunodeficiency virus (HIV) nucleocapsid protein (NCp) with a substrate closely mimicking a retrovirus replication intermediate was studied. The heteroduplex substrate consisted of a DNA and RNA of 80 and 63 nucleotides, respectively. The nucleotides at the 3' end of the DNA were complementary to those at the 3' end of the RNA such that a hybrid region of 30 base pairs could form. HIV-reverse transcriptase (RT) extended the DNA and cleaved the RNA strand of the substrate. The rates of extension and cleavage were significantly decreased when the substrate was prebound with NCp before HIV-RT addition. In assays assessing the integrity of the substrate by measuring release of the DNA strand from the heteroduplex, prebinding with NCp protected the substrate when HIV-RT was added, a result consistent with resistance to RT-mediated cleavage. In contrast, NCp significantly decreased the thermal stability of the substrate as judged by incubation of the substrate at various temperatures. In strand transfer assays, a 189-nucleotide RNA (acceptor) with an internal region complementary to all 80 nucleotides of the substrate DNA was incubated with the substrate in the presence or absence of NCp. Nucleocapsid protein stimulated strand transfer in which the substrate RNA was displaced upon binding of the DNA to the acceptor. Results are discussed with respect to the role of NCp in retroviral recombination.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

Publication types

LinkOut - more resources