ArticleEukaryotic cell2005
Role of integrase in reverse transcription of the Saccharomyces cerevisiae retrotransposon Ty1.
Article in Eukaryotic cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition.Mobile DNA · 2022Article
- Ty1 integrase is composed of an active N-terminal domain and a large disordered C-terminal module dispensable for its activity in vitro.The Journal of biological chemistry · 2021Article
- A small targeting domain in Ty1 integrase is sufficient to direct retrotransposon integration upstream of tRNA genes.The EMBO journal · 2020Article
- The Ty1 LTR-retrotransposon of budding yeast,Microbiology spectrum · 2015Article
- Exploring Ty1 retrotransposon RNA structure within virus-like particles.Nucleic acids research · 2013Article
- The removal of RNA primers from DNA synthesized by the reverse transcriptase of the retrotransposon Tf1 is stimulated by Tf1 integrase.Journal of virology · 2012Article
- Posttranslational interference of Ty1 retrotransposition by antisense RNAs.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Functional analysis of N-terminal residues of ty1 integrase.Journal of virology · 2009Article
- The diversity of retrotransposons and the properties of their reverse transcriptases.Virus research · 2008Review
- Mn2+ suppressor mutations and biochemical communication between Ty1 reverse transcriptase and RNase H domains.Journal of virology · 2007Article
- Cooperation between reverse transcriptase and integrase during reverse transcription and formation of the preintegrative complex of Ty1.Eukaryotic cell · 2006Article
- Revealing domain structure through linker-scanning analysis of the murine leukemia virus (MuLV) RNase H and MuLV and human immunodeficiency virus type 1 integrase proteins.Journal of virology · 2006Article
- The self primer of the long terminal repeat retrotransposon Tf1 is not removed during reverse transcription.Journal of virology · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reverse transcriptase (RT) with its associated RNase H (RH) domain and integrase (IN) are key enzymes encoded by retroviruses and retrotransposons. Several studies have implied a functional role of the interaction between IN and RT during the replication of retroviral and retrotransposon genomes. In this study, IN deletion mutants were used to investigate the role of IN on the RT activity of the yeast Saccharomyces cerevisiae retrotransposon Ty1. We have identified two domains of Ty1 integrase which have effects on RT activity in vivo. The deletion of a domain spanning amino acid residues 233 to 520 of IN increases the exogenous specific activity of RT up to 20-fold, whereas the removal of a region rich in acidic amino acid residues between residues 521 and 607 decreases its activity. The last result complements our observation that an active recombinant RT protein can be obtained if a small acidic tail mimicking the acidic domain of IN is fused to the RT-RH domain. We suggest that interaction between these acidic amino acid residues of IN and a basic region of RT could be critical for the correct folding of RT and for the formation of an active conformation of the enzyme.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.