A nucleocapsid functionality contained within the amino terminus of the ty1 protease that is distinct and separable from proteolytic activity

Jr Lawler J.F., G. V. Merkulov, J. D. Boeke

Research output: Contribution to journalArticle

Abstract

Ty1 is the most successful of the five endogenous yeast retrotransposons. The life cycle of Ty1 dictates that a number of nucleocapsid (NC)-facilitated events occur although the protein(s) responsible for these events has not been identified. The positioning of the NC peptide is conserved at the carboxy terminus of the Gag protein among most long terminal repeat (LTR)-containing retroelements. An analogous region of Ty1 that simultaneously encodes part of Gag, protease (PR), and the C-terminal p4 peptide was mutagenized. Some of these mutations result in smaller-than-normal virus-like particles (VLPs). The mutants were also found to impair an NC-like functionality contained within the amino terminus of the protease that is distinct and separable from its proteolytic activity. Remarkably, these mutants have distinct defects in reverse transcription.

Original languageEnglish (US)
Pages (from-to)346-354
Number of pages9
JournalJournal of Virology
Volume76
Issue number1
DOIs
StatePublished - 2002

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Nucleocapsid
nucleocapsid
Retroelements
Peptide Hydrolases
proteinases
retrotransposons
peptides
gag Gene Products
mutants
terminal repeat sequences
reverse transcription
virus-like particles
Terminal Repeat Sequences
Life Cycle Stages
Virion
Reverse Transcription
life cycle (organisms)
proteins
Yeasts
yeasts

ASJC Scopus subject areas

  • Immunology

Cite this

A nucleocapsid functionality contained within the amino terminus of the ty1 protease that is distinct and separable from proteolytic activity. / Lawler J.F., Jr; Merkulov, G. V.; Boeke, J. D.

In: Journal of Virology, Vol. 76, No. 1, 2002, p. 346-354.

Research output: Contribution to journalArticle

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