Interaction of Human Immunodeficiency Virus Nucleocapsid Protein with a Structure Mimicking a Replication Intermediate EFFECTS ON STABILITY, REVERSE TRANSCRIPTASE BINDING, AND STRAND TRANSFER

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