Proteolytic processing of Ty3 proteins is required for transposition.
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Determinants of Genomic RNA Encapsidation in the Saccharomyces cerevisiae Long Terminal Repeat Retrotransposons Ty1 and Ty3Ty3 capsid mutations reveal early and late functions of the amino-terminal domainInvestigation by atomic force microscopy of the structure of Ty3 retrotransposon particles.A single zinc finger optimizes the DNA interactions of the nucleocapsid protein of the yeast retrotransposon Ty3.Schizosaccharomyces pombe retrotransposon Tf2 mobilizes primarily through homologous cDNA recombination.Proteolytic processing and assembly of gag and gag-pol proteins of TED, a baculovirus-associated retrotransposon of the gypsy family.A map of interactions between the proteins of a retrotransposonTen-kilodalton domain in Ty3 Gag3-Pol3p between PR and RT is dispensable for Ty3 transposition.Expression and processing of proteins encoded by the Saccharomyces retrotransposon Ty5The yeast Ty3 retrotransposon contains a 5'-3' bipartite primer-binding site and encodes nucleocapsid protein NCp9 functionally homologous to HIV-1 NCp7A rare tRNA-Arg(CCU) that regulates Ty1 element ribosomal frameshifting is essential for Ty1 retrotransposition in Saccharomyces cerevisiaeTy3 transposes in mating populations of yeast: a novel transposition assay for Ty3Ty3 integrase is required for initiation of reverse transcriptionConvergent evolution of ribonuclease h in LTR retrotransposons and retroviruses.The diversity of retrotransposons and the properties of their reverse transcriptases.The TY3 Gag3 spacer controls intracellular condensation and uncoatingFunction of a retrotransposon nucleocapsid proteinA long terminal repeat-containing retrotransposon of Schizosaccharomyces pombe expresses a Gag-like protein that assembles into virus-like particles which mediate reverse transcription.Characterization of a nucleocapsid-like region and of two distinct primer tRNALys,2 binding sites in the endogenous retrovirus Gypsy.Ty3 Retrotransposon Hijacks Mating Yeast RNA Processing Bodies to Infect New Genomes.A critical proteolytic cleavage site near the C terminus of the yeast retrotransposon Ty1 Gag protein.Ty3 nucleocapsid controls localization of particle assemblyThe retrotransposon Tf1 assembles virus-like particles that contain excess Gag relative to integrase because of a regulated degradation processSequence requirements for localization and packaging of Ty3 retroelement RNA.Transposition of the yeast retroviruslike element Ty3 is dependent on the cell cycleNucleocapsid protein function in early infection processes.The chromodomain of Tf1 integrase promotes binding to cDNA and mediates target site selection.Using pyrrolo-deoxycytosine to probe RNA/DNA hybrids containing the human immunodeficiency virus type-1 3' polypurine tract.Cellular stress inhibits transposition of the yeast retrovirus-like element Ty3 by a ubiquitin-dependent block of virus-like particle formation.Reverse Transcription in the Saccharomyces cerevisiae Long-Terminal Repeat Retrotransposon Ty3.Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein.Mutations in nonconserved domains of Ty3 integrase affect multiple stages of the Ty3 life cycleTy1 proteolytic cleavage sites are required for transposition: all sites are not created equal.An active-site mutation in the human immunodeficiency virus type 1 proteinase (PR) causes reduced PR activity and loss of PR-mediated cytotoxicity without apparent effect on virus maturation and infectivityMutations in the Ty3 major homology region affect multiple steps in Ty3 retrotransposition.Ty3 integrase mutants defective in reverse transcription or 3'-end processing of extrachromosomal Ty3 DNA.The Cys-His motif of Ty3 NC can be contributed by Gag3 or Gag3-Pol3 polyproteins.Role of integrase in reverse transcription of the Saccharomyces cerevisiae retrotransposon Ty1.Convergent evolution of integration site selection upstream of tRNA genes by yeast and amoeba retrotransposons
P2860
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P2860
Proteolytic processing of Ty3 proteins is required for transposition.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Proteolytic processing of Ty3 proteins is required for transposition.
@en
type
label
Proteolytic processing of Ty3 proteins is required for transposition.
@en
prefLabel
Proteolytic processing of Ty3 proteins is required for transposition.
@en
P2860
P1433
P1476
Proteolytic processing of Ty3 proteins is required for transposition.
@en
P2093
J Kirchner
S Sandmeyer
P2860
P407
P577
1993-01-01T00:00:00Z