Adaptation of the molecular level: comparative molecular study of interstitial collagens from coastal (Arenicola marina) and hydrothermal vent (Alvinella pompejana) polychaetous annelids
Sicot, F.-X.; Deutsch, J.; Masselot, M.; Gaill, F. (1997). Adaptation of the molecular level: comparative molecular study of interstitial collagens from coastal (Arenicola marina) and hydrothermal vent (Alvinella pompejana) polychaetous annelids, 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. 142
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; e-ISSN 2262-3094, more
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| Authors | | Top |
- Sicot, F.-X.
- Deutsch, J.
- Masselot, M.
- Gaill, F.
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| Abstract |
The polychaete Alvinella pompejana is probably the most heat-tolerant metazoan organism. Previous observations have shown that the thermal stability of this species was significantly greater than that of the coastal annelid Arenicola marina, or than that of the vestimentiferan Riftia pachyptila, a species living in a colder part of the hydrothermal vent environment. We investigated the molecular basis of this adaptation. We cloned and sequenced a cDNA coding the fibrillar collagens of both lugworm and alvinellid species. The fragments obtained include approximately one half of the helical-domain of these collagens, along with the entire C-propeptide domain which is processed outside the cell. Analysis of the evolution of the C-propeptide shows strong evolutive constraints, fitting well with a previously formulated hypothesis concerning the role of this molecular domain in triggering trimerization process of the collagens. Comparison of the helical-corresponding domains in these species (including that of Riftia pachyptila, which had been previously obtained using other methods) allows us to hypothesize on the precise nature of major factors which account for the thermal stability of alvinellid collagen. In particular, the abundance of Proline-rich triplets seems to pinpoint the important role of this amino acid. Other sites were also reported. Our future goal is to experimentally test the effect of these sites, by producing "mutant" recombinant proteins by genetic engeneering. |
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