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  <title>DSpace Collection:</title>
  <link rel="alternate" href="http://hdl.handle.net/10362/3724" />
  <subtitle />
  <id>http://hdl.handle.net/10362/3724</id>
  <updated>2013-05-26T06:27:22Z</updated>
  <dc:date>2013-05-26T06:27:22Z</dc:date>
  <entry>
    <title>Novel Secretion Apparatus Maintains Spore Integrity and Developmental Gene&#xD;
Expression in Bacillus subtilis</title>
    <link rel="alternate" href="http://hdl.handle.net/10362/5842" />
    <author>
      <name>Doan, T.</name>
    </author>
    <author>
      <name>Morlot, C.</name>
    </author>
    <author>
      <name>Meisner, J.</name>
    </author>
    <author>
      <name>Serrano, M.</name>
    </author>
    <author>
      <name>Henriques, A. O.</name>
    </author>
    <author>
      <name>Moran, C. P.</name>
    </author>
    <author>
      <name>Rudner, D. Z.</name>
    </author>
    <id>http://hdl.handle.net/10362/5842</id>
    <updated>2011-06-28T15:18:00Z</updated>
    <published>2009-01-01T00:00:00Z</published>
    <summary type="text">Title: Novel Secretion Apparatus Maintains Spore Integrity and Developmental Gene&#xD;
Expression in Bacillus subtilis
Authors: Doan, T.; Morlot, C.; Meisner, J.; Serrano, M.; Henriques, A. O.; Moran, C. P.; Rudner, D. Z.
Abstract: Sporulation in Bacillus subtilis involves two cells that follow separate but&#xD;
coordinately regulated developmental programs. Late in sporulation, the&#xD;
developing spore (the forespore) resides within a mother cell. The regulation of&#xD;
the forespore transcription factor sigma(G) that acts at this stage has remained&#xD;
enigmatic. sigma(G) activity requires eight mother-cell proteins encoded in the&#xD;
spoIIIA operon and the forespore protein SpoIIQ. Several of the SpoIIIA proteins&#xD;
share similarity with components of specialized secretion systems. One of them&#xD;
resembles a secretion ATPase and we demonstrate that the ATPase motifs are&#xD;
required for sigma(G) activity. We further show that the SpoIIIA proteins and&#xD;
SpoIIQ reside in a multimeric complex that spans the two membranes surrounding&#xD;
the forespore. Finally, we have discovered that these proteins are all required&#xD;
to maintain forespore integrity. In their absence, the forespore develops large&#xD;
invaginations and collapses. Importantly, maintenance of forespore integrity&#xD;
does not require sigma(G). These results support a model in which the SpoIIIA-&#xD;
SpoIIQ proteins form a novel secretion apparatus that allows the mother cell to&#xD;
nurture the forespore, thereby maintaining forespore physiology and sigma(G)&#xD;
activity during spore maturation.
Description: Plos Genetics, 5(7): ARTe1000566</summary>
    <dc:date>2009-01-01T00:00:00Z</dc:date>
  </entry>
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