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Article

A Ty1 reverse transcriptase active-site aspartate mutation blocks transposition but not polymerization.

Journal of virology - 1 Jul 2001

Uzun O, Gabriel A

Abstract excerpt

Reverse transcriptases (RTs) are found in a wide variety of mobile genetic elements including viruses, retrotransposons, and infectious organellar introns. An invariant triad of aspartates is thought to be required for the catalytic function of RTs. We generated RT mutants in the yeast retrotransposon Ty1, changing each of these active-site aspartates to asparagine or glutamate. All but one of the mutants lacked...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 11413300
DOI: 10.1128/JVI.75.14.6337-6347.2001
PMCID: PMC114356

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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A Ty1 reverse transcriptase active-site aspartate mutation blocks transposition but not polymerization.PMID 11413300Read ↗

Replication infidelity during a single cycle of Ty1 retrotransposition.Semantic proximity Read ↗

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Interaction of the Ty3 reverse transcriptase thumb subdomain with template-primer.Semantic proximity Read ↗

A nucleocapsid functionality contained within the amino terminus of the Ty1 protease that is distinct and separable from proteolytic activity.Semantic proximity Read ↗

Novel transcript truncating function of Rap1p revealed by synthetic codon-optimized Ty1 retrotransposon.Semantic proximity Read ↗

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Plus-strand strong-stop DNA synthesis in retrotransposon Ty1.Semantic proximity Read ↗

The central PPT of the yeast retrotransposon Ty1 is not essential for transposition.Semantic proximity Read ↗

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