Document 0502
 DOCN  M9480502
 TI    Characterization of human immunodeficiency virus type 1 dimeric RNA from
       wild-type and protease-defective virions.
 DT    9410
 AU    Fu W; Gorelick RJ; Rein A; ABL-Basic Research Program, NCI-Frederick
       Cancer Research and; Development Center, Maryland 21702-1201.
 SO    J Virol. 1994 Aug;68(8):5013-8. Unique Identifier : AIDSLINE
       MED/94309166
 AB    We have characterized the dimeric genomic RNA in particles of both
       wild-type and protease (PR)-deficient human immunodeficiency virus type
       1 (HIV-1). We found that the dimeric RNA isolated from PR- mutant
       virions has a lower mobility in nondenaturing gel electrophoresis than
       that from wild-type virions. It also dissociates into monomers at a
       lower temperature than the wild-type dimer. Thus, the dimer in PR-
       particles is in a conformation different from that in wild-type
       particles. These results are quite similar to recent findings on Moloney
       murine leukemia virus and suggest that a postassembly, PR-dependent
       maturation event is a common feature in genomic RNAs of retroviruses. We
       also measured the thermal stability of the wild-type and PR- dimeric
       RNAs under different ionic conditions. Both forms of the dimer were
       stabilized by increasing Na+ concentrations. However, the melting
       temperatures of the two forms were not significantly affected by the
       identity of the monovalent cation present in the incubation buffer. This
       observation is in contrast with recent reports on dimers formed in vitro
       from short segments of HIV-1 sequence: the latter dimers are
       specifically stabilized by K+ ions. K+ stabilization of dimers formed in
       vitro has been taken as evidence for the presence of guanine quartet
       structures. The results suggest that guanine quartets are not involved
       in the structure linking full-length, authentic genomic RNA of HIV-1
       into a dimeric structure.
 DE    Biopolymers  Hela Cells  Human  HIV Protease/*METABOLISM
       HIV-1/ENZYMOLOGY/*GENETICS  Nucleic Acid Conformation  RNA,
       Viral/*CHEMISTRY  Sodium Chloride  Support, U.S. Gov't, P.H.S.
       Temperature  Virion/ENZYMOLOGY/GENETICS  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).