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The enzymes of synthesis and utilization of carbamylphosphate in the deep-sea tubeworm Riftia pachyptila an its bacterial symbiont
Simon, V.; Purcarea, C.; Sun, K.; Joseph, J.; Gaill, F.; Herve, G. (1997). The enzymes of synthesis and utilization of carbamylphosphate in the deep-sea tubeworm Riftia pachyptila an its bacterial symbiont, in: Biologie des sources hydrothermales profondes = Biology of deep-sea hydrothermal vents: Journées d'échanges du Programme DORSALES = DORSALES Workshop Roscoff 6-8 octobre 1997. Cahiers de Biologie Marine, 38(2): pp. 143
In: (1997). Biologie des sources hydrothermales profondes = Biology of deep-sea hydrothermal vents: Journées d'échanges du Programme DORSALES = DORSALES Workshop Roscoff 6-8 octobre 1997. Cahiers de Biologie Marine, 38(2)[s.n.][s.l.]. 111-149 pp., more
In: Cahiers de Biologie Marine. Station Biologique de Roscoff: Paris. ISSN 0007-9723, more
Peer reviewed article  

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Keyword
    Marine

Authors  Top 
  • Simon, V.
  • Purcarea, C.
  • Sun, K.
  • Joseph, J.
  • Gaill, F.
  • Herve, G.

Abstract
    To investigate metabolic implications of the symbiosis between the giant tubeworm Riftia pachyptila and its bacterial symbiont, we studied the presence of three enzymes involved in the synthesis and utilization of carbamylphosphate: Carbamylphosphate Synthetase (CPSase), Aspartate Transcarbamylase (ATCase) and Omithine Transcarbamylase (OTCase). Five different parts of the worm were investigated: the plume, the vestimentum, the body wall, the trophosome and the opisthosome.CPSase, which synthesizes the carbamylphosphate, was mainly detected in the trophosome and some residual activity could be measured in the other organs. OTCase, which uses carbamylphosphate in the arginine biosynthesis pathway, was homogeneously distributed in the different parts of the worm. On the contrary, ATCase, which uses carbamylphosphate in the pyrimidine biosynthesis pathway, was only detected in the trophosome, the unique organ where the bacterial symbionts are present. However, no ATCase activity was measured in the isolated bacteria. Thus, pyrimidine nucleotides might be provided to bacteria by the Riftia worm, in agreement with the impossibility to grow isolated bacteria in culture media. Nevertheless, we cannot exclude that bacterial enzyme, with very different characteristics from previously described ATCases, remains undetected under our test conditions.

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