Publications by authors named "Heidi Olivares"

Severe acute respiratory syndrome coronavirus encodes several accessory proteins of unknown function. We previously showed that one such protein, encoded by ORF6, enhanced the growth of mouse hepatitis virus in tissue culture cells and in mice. Protein 6 consists of an N-terminal hydrophobic peptide and a C-terminal region containing intracellular protein sorting motifs.

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One or more of the unique 3'-proximal open reading frames (ORFs) of the severe acute respiratory syndrome (SARS) coronavirus may encode determinants of virus virulence. A prime candidate is ORF6, which encodes a 63-amino-acid membrane-associated peptide that can dramatically increase the lethality of an otherwise attenuated JHM strain of murine coronavirus (L. Pewe, H.

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The meiosis-specific recombinase Dmc1 plays a critical role in DNA strand exchange in budding yeast. Tid1/Rdh54, a member of the Swi2/Snf2 family of DNA translocases, has been shown to stimulate Dmc1-dependent recombination. Tid1and its budding yeast paralog Rad54 have a variety of biochemical activities that may contribute to their biological function.

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Most animal species that can be infected with the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) do not reproducibly develop clinical disease, hindering studies of pathogenesis. To develop an alternative system for the study of SARS-CoV, we introduced individual SARS-CoV genes (open reading frames [ORFs]) into the genome of an attenuated murine coronavirus. One protein, the product of SARS-CoV ORF6, converted a sublethal infection to a uniformly lethal encephalitis and enhanced virus growth in tissue culture cells, indicating that SARS-CoV proteins function in the context of a heterologous coronavirus infection.

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Article Synopsis
  • Saccharomyces cerevisiae Hop2 and Mnd1 are crucial proteins for meiosis, with mutations causing issues in chromosome interactions and recombination.
  • Analyses of double mutants reveal that HOP2, MND1, and DMC1 operate in the same pathway to facilitate the close pairing of homologous chromosomes during meiosis.
  • Biochemical experiments show that Hop2 and Mnd1 form a heterodimer that binds more effectively to double-stranded DNA and enhances Dmc1's strand assimilation activity, indicating their interdependence in meiotic DNA recombination.
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