Identification of sites that act together to direct dimerization of human foamy virus RNA in vitro.
Retroviral particles contain two molecules of genomic RNA, which are noncovalently linked near their 5' ends in a region called the dimer linkage structure (DLS). By using complementary DNA oligonucleotides and deletion mutants to impair RNA dimerization of the human foamy virus (HFV), three sites, designated SI, SII, and SIII, were found within a 159-nucleotide RNA fragment of HFV that are involved in dimerization in vitro. SI overlaps the primer-binding site; and SII contains the palindromic sequence, UCCCUAGGGA, the disruption of which impairs dimer formation; and SIII extends into the gag gene. The first two sites are highly conserved in the other primate foamy viruses, SFV-1, SFV-3, and SFVcpz, whereas the third appears to be shared only by HFV and SFVcpz. RNA of HFV and SFV-3 could form heterodimers, indicating that both viruses dimerize by similar mechanisms. On testing thermal stability, dimers of the 159-nucleotide fragment dissociated between 40 and 70 degrees, with half of the dimers dissociating at 55 degrees. Since the splice donor site of HFV is located at position 51 of viral RNA, the DLS is part of the genomic RNA exclusively.
Erlwein
O
O
Department of Genito-Urinary Medicine & Communicable Diseases, Jefferiss Research Trust Laboratories, Imperial College School of Medicine at St. Mary's, London, United Kingdom.
Cain
D
D
Fischer
N
N
Rethwilm
A
A
McClure
M O
MO
D001665:Binding Sites; D001704:Biopolymers; D018076:DNA, Complementary; D006358:Hot Temperature; D012367:RNA, Viral / Q000235:genetics / Q000378:metabolism*; D015183:Restriction Mapping; D017384:Sequence Deletion; D016092:Spumavirus / Q000235:genetics*
D001704:Biopolymers; D018076:DNA, Complementary; D012367:RNA, Viral