Martin-Rendon E, Hurd D W, Marfany G, Kingsman S M, Kingsman A J
Department of Biochemistry, University of Oxford, UK.
Mol Microbiol. 1996 Dec;22(5):1035-43. doi: 10.1046/j.1365-2958.1996.01544.x.
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.
