Abstract
Limited proteolysis is a well-established posttranslational mechanism by which cellular and viral precursor proteins are cleaved by specific proteinases into functional species (Koch and (Richter 1980). Examples of such cellular proteins are the neuropolypeptide prohormones (Mains et al. 1983) and propiocortin, while the best known viral polyproteins are the polio (Summers and Maizel 1968; Jacobson and Baltimore 1968) and retroviral gag and gag-pol encoded polyproteins (Dickson et al. 1984). Two recent reviews during the past year have focused on viral proteinases coded for by positive-strand RNA viruses e.g., picorna and toga-flavivirus families (Kräusslich and Wimmer 1988), or by plant viruses (Wellink and van Kammen 1988). The focus of this review will be on a discussion of the biochemical properties as well as functions of retroviral proteinases (PR). These enzymes cleave both gag and gag-pol encoded polyproteins (cleavage of the env encoded polyprotein occurs via a cellular Golgilocalized enzyme).
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Oroszlan, S., Luftig, R.B. (1990). Retroviral Proteinases. In: Swanstrom, R., Vogt, P.K. (eds) Retroviruses. Current Topics in Microbiology and Immunology, vol 157. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75218-6_6
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