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

Molecular Microbiology
E Martin-RendonA J Kingsman

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.

Citations

Jun 16, 2005·Journal of Virology·Yurii G KuznetsovSuzanne Sandmeyer
Aug 12, 2005·Cytogenetic and Genome Research·F-X WilhelmA Gabriel
Nov 2, 2002·Molecular Biology and Evolution·Brooke D Peterson-Burch, Daniel F Voytas
Aug 31, 2019·RNA Biology·Julita GumnaKatarzyna Pachulska-Wieczorek
Jun 22, 2000·Yeast·J F Roth

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