Identification of proteolytic cleavage sites within the gag-analogue protein of Ty1 virus-like particles.
Like retroviruses, the yeast retrotransposon Ty1 produces its proteins as precursors that are subsequently cleaved by a protease encoded by the element. These cleavage events are essential for transposition as they release the active reverse transcriptase and integrase and they modify the structure of the virus-like particles in a way that is analogous to the morphological changes that occur during retrovirus core maturation. Using a combination of epitope tagging, amino acid analysis and mutagenesis, we have identified the major cleavage sites for the Ty1 protease within the particle-forming protein, p1, at 407S/408N. In addition, we present evidence indicating that the Ty1 protease may be a 17 kDa protein.
Martin-Rendon
E
E
Department of Biochemistry, University of Oxford, UK.
Hurd
D W
DW
Marfany
G
G
Kingsman
S M
SM
Kingsman
A J
AJ
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism; D001665:Binding Sites; D010450:Endopeptidases / Q000378:metabolism*; D000939:Epitopes; D005800:Genes, Fungal; D015750:Genes, gag; D006801:Humans; D008969:Molecular Sequence Data; D018626:Retroelements; D012441:Saccharomyces cerevisiae / Q000235:genetics*
D000939:Epitopes; D018626:Retroelements; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases