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  • 1
    Online Resource
    Online Resource
    Elsevier BV ; 1998
    In:  Experimental Cell Research Vol. 242, No. 1 ( 1998-07), p. 265-273
    In: Experimental Cell Research, Elsevier BV, Vol. 242, No. 1 ( 1998-07), p. 265-273
    Type of Medium: Online Resource
    ISSN: 0014-4827
    RVK:
    Language: English
    Publisher: Elsevier BV
    Publication Date: 1998
    detail.hit.zdb_id: 1466780-0
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 1996
    In:  Genetics Vol. 143, No. 3 ( 1996-07-01), p. 1057-1068
    In: Genetics, Oxford University Press (OUP), Vol. 143, No. 3 ( 1996-07-01), p. 1057-1068
    Abstract: Many group I introns encode endonucleases that promote intron homing by initiating a double-strand break-mediated homologous recombination event. A td intron-phage λ model system was developed to analyze exon homology effects on intron homing and determine the role of the λ 5′–3′ exonuclease complex (Redαβ) in the repair event. Efficient intron homing depended on exon lengths in the 35- to 50-bp range, although homing levels remained significantly elevated above nonbreak-mediated recombination with as little as 10 bp of flanking homology. Although precise intron insertion was demonstrated with extremely limiting exon homology, the complete absence of one exon produced illegitimate events on the side of heterology. Interestingly, intron inheritance was unaffected by the presence of extensive heterology at the double-strand break in wild-type λ, provided that sufficient homology between donor and recipient was present distal to the heterologous sequences. However, these events involving heterologous ends were absolutely dependent on an intact Red exonuclease system. Together these results indicate that heterologous sequences can participate in double-strand break-mediated repair and imply that intron transposition to heteroallelic sites might occur at break sites within regions of limited or no homology.
    Type of Medium: Online Resource
    ISSN: 1943-2631
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 1996
    detail.hit.zdb_id: 1477228-0
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    American Society for Microbiology ; 1999
    In:  Journal of Virology Vol. 73, No. 5 ( 1999-05), p. 4524-4529
    In: Journal of Virology, American Society for Microbiology, Vol. 73, No. 5 ( 1999-05), p. 4524-4529
    Abstract: Several viruses, including members of the gammaherpesvirus family, encode proteins that are secreted into the extracellular environment. We have identified an abundant 44-kDa secreted protein that is present in the supernatant of fibroblasts infected with murine gammaherpesvirus 68 (γHV68; also referred to as MHV-68) but not in that of uninfected fibroblasts. Sequence analysis of the amino terminus and of internal peptides revealed that this protein is encoded by the γHV68 M3 open reading frame (ORF). The amino-terminal sequence of the secreted protein starts at residue 25 of the M3 ORF, consistent with the first 24 residues functioning as a signal peptide. Northern blot analysis revealed a single abundant ∼1.4-kb early-late lytic transcript encoded by the M3 ORF. Analysis of a partial cDNA clone and subsequent analyses of products of rapid amplification of cDNA ends coupled with S1 nuclease protection assays demonstrate that the M3 protein is encoded by an unspliced, polyadenylated mRNA initiating at bp 7294 and terminating at bp 6007 of the γHV68 genome. The 3′ end of the M3 transcript maps 9 bp downstream of a consensus polyadenylation signal. Thus, the predicted M3 ORF is a functional gene that encodes an abundant secreted protein which is a candidate for interacting with host cellular receptors or cytokines.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1999
    detail.hit.zdb_id: 1495529-5
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  • 4
    Online Resource
    Online Resource
    American Society for Microbiology ; 2005
    In:  Journal of Bacteriology Vol. 187, No. 22 ( 2005-11-15), p. 7805-7814
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 187, No. 22 ( 2005-11-15), p. 7805-7814
    Abstract: Previously, we conducted a mutant screen of Pseudomonas syringae pv. tomato strain DC3000 to identify genes that contribute to virulence on Arabidopsis thaliana plants. Here we describe the characterization of one mutant strain, DB4H2, which contains a single Tn 5 insertion in PSPTO3576, an open reading frame that is predicted to encode a protein belonging to the TetR family of transcriptional regulators. We demonstrate that PSPTO3576 is necessary for virulence in DC3000 and designate the encoded protein TvrR ( T etR-like v i r ulence r egulator). TvrR, like many other TetR-like transcriptional regulators, negatively regulates its own expression. Despite the presence of a putative HrpL binding site in the tvrR promoter region, tvrR is not regulated by HrpL, an alternative sigma factor that regulates the expression of many known DC3000 virulence genes. tvrR mutant strains grow comparably to wild-type DC3000 in culture and possess an intact type III secretion system. However, tvrR mutants do not cause disease symptoms on inoculated A. thaliana and tomato plants, and their growth within plant tissue is significantly impaired. We demonstrate that tvrR mutant strains are able to synthesize coronatine (COR), a phytotoxin required for virulence of DC3000 on A. thaliana . Given that tvrR mutant strains are not defective for type III secretion or COR production, tvrR appears to be a novel virulence factor required for a previously unexplored process that is necessary for pathogenesis.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2005
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    Wiley ; 1996
    In:  Molecular Microbiology Vol. 21, No. 6 ( 1996-10), p. 1219-1225
    In: Molecular Microbiology, Wiley, Vol. 21, No. 6 ( 1996-10), p. 1219-1225
    Type of Medium: Online Resource
    ISSN: 0950-382X , 1365-2958
    Language: English
    Publisher: Wiley
    Publication Date: 1996
    detail.hit.zdb_id: 1501537-3
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