Ribosomal frameshifting at the Gag-Pol junction in avian leukemia sarcoma virus forms a novel cleavage site.
The Gag and Gag-Pol precursors of avian sarcoma leukemia virus (ASLV) are translated from viral genomic-size mRNA at a molar ratio of about 20:1. Translation of Gag is terminated at the stop codon UAG located at the carboxyl-terminus of the viral protease (PR), whereas a ribosomal frameshift occurring at the carboxyl-terminus of Gag allows translation of the Gag-Pol precursor. To determine how PR is released from the Gag-Pol precursor, a single base (A or T) was inserted at the Gag-Pol junction in order to adjust the translation into a single reading frame. These mutations allow processing of the viral precursor when expressed in bacterial cells, but cause cessation of viral production after transfection of avian cells. The viral PR released from the large precursor is one amino acid longer than PR cleaved from the Gag polyprotein and is terminated by an Ile instead of a Leu residue.
Arad
G
G
Department of Molecular Genetics, Hebrew University, Hadassah Medical School, Jerusalem, Israel.
Bar-Meir
R
R
Kotler
M
M
D001355:Alpharetrovirus / Q000235:genetics* / Q000254:growth & development; D000595:Amino Acid Sequence; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics; D015685:Fusion Proteins, gag-pol / Q000096:biosynthesis / Q000235:genetics*; D008969:Molecular Sequence Data; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D016364:Reading Frames / Q000235:genetics*; D011994:Recombinant Proteins; D012270:Ribosomes / Q000378:metabolism*
D015685:Fusion Proteins, gag-pol; D011994:Recombinant Proteins