Identification of proteolytic cleavage sites within the gag-analogue protein of Ty1 virus-like particles

Authors: Martin-Rendon, Enca¹; Hurd, Douglas W.¹; Marfany, Gemma¹; Kingsman, Susan M.¹; Kingsman, Alan J.¹

Source: Molecular Microbiology, Volume 22, Number 5, December 1996 , pp. 1035-1043(9)

Publisher: Blackwell Publishing

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Abstract:

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.

Document Type: Research article

DOI: 10.1046/j.1365-2958.1996.01544.x

Affiliations: 1: Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.

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