Positionally independent and exchangeable late budding functions of the Rous sarcoma virus and human immunodeficiency virus Gag proteins.
The Gag proteins of Rous sarcoma virus and human immunodeficiency virus (HIV) each contain a function involved in a late step in budding, defects in which result in the accumulation of these molecules at the plasma membrane. In the Rous sarcoma virus Gag protein (Pr76gag), this assembly domain is associated with a PPPY motif, which is located at an internal position between the MA and CA sequences. This motif is not contained anywhere within the HIV Gag protein (Pr55gag), and the MA sequence is linked directly to CA. Instead, a late assembly function of HIV has been associated with the p6 sequence situated at the C terminus of Gag. Here we demonstrate the remarkable finding that the late assembly domains from these two unrelated Gag proteins are exchangeable between retroviruses and can function in a positionally independent manner.
Parent
L J
LJ
Department of Microbiology and Immunology, Pennsylvania State University College of Medicine, Hershey 17033, USA.
Bennett
R P
RP
Craven
R C
RC
Nelle
T D
TD
Krishna
N K
NK
Bowzard
J B
JB
Wilson
C B
CB
Puffer
B A
BA
Montelaro
R C
RC
Wills
J W
JW
D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D001358:Avian Sarcoma Viruses / Q000502:physiology*; D001483:Base Sequence; D002460:Cell Line; D002522:Chlorocebus aethiops; D003001:Cloning, Molecular; D017931:DNA Primers; D015683:Gene Products, gag / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism*; D015750:Genes, gag; D006678:HIV / Q000502:physiology*; D007668:Kidney; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D014162:Transfection
D017931:DNA Primers; D015683:Gene Products, gag; D011994:Recombinant Proteins