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Comparison of proton-specific ATPase activities in plume and root tissues of two co-occurring hydrocarbon seep tubeworm species Lamellibrachia luymesi and Seepiophila jonesi
Dattagupta, S.; Redding, M.; Luley, K.; Fisher, C. (2009). Comparison of proton-specific ATPase activities in plume and root tissues of two co-occurring hydrocarbon seep tubeworm species Lamellibrachia luymesi and Seepiophila jonesi. Mar. Biol. (Berl.) 156(4): 779-786. http://hdl.handle.net/10.1007/s00227-009-1132-2
In: Marine Biology. Springer: Heidelberg; Berlin. ISSN 0025-3162, more
Peer reviewed article  

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Keyword
    Marine

Authors  Top 
  • Dattagupta, S.
  • Redding, M.
  • Luley, K.
  • Fisher, C.

Abstract
    Lamellibrachia luymesi and Seepiophila jonesi are co-occurring species of vestimentiferan tubeworms found at hydrocarbon seepage sites on the upper Louisiana slope of the Gulf of Mexico. Like all vestimentiferans, they rely on internal sulfide-oxidizing symbiotic bacteria for nutrition. These symbionts produce hydrogen ions as a byproduct of sulfide oxidation, which the host tubeworm needs to eliminate to prevent acidosis. The hydrothermal vent tubeworm Riftia pachyptila uses a high activity of P- and V-type H+-ATPases located in its plume epithelium to excrete protons. Unlike R. pachyptila, the seep species grow a posterior root, which they can use in addition to their plumes as a nutrient exchange surface. In this study we measured the ATPase activities of plume and root tissues collected from L. luymesi and S. jonesi, and used a combination of inhibitors to determine the relative activities of P- and V-type H+-ATPases. We found that the total H+-ATPase activity of their plumes was approximately 14 µmol h-1 g-1 wet weight, and that of their roots was between 5 and 7 µmol h-1 g-1 wet weight. These activities were more than ten times lower than those measured in R. pachyptila. We suggest that seep tubeworms might use passive channels to eliminate protons across their roots, in addition to ATP-dependant proton pumps located in their plumes and roots. In addition, we found strong differences between the types of ATPase activities in the plumes of L. luymesi and S. jonesi. While the H+-ATPase activity of L. luymesi plumes is dominated by P-type ATPases, S. jonesi has an unusually high activity of V-type H+-ATPases. We suggest that S. jonesi relies on its high V-type H+-ATPase activity to drive carbon dioxide uptake across its plume surface. L. luymesi, on the other hand, might rely partially on bicarbonate uptake across its root.

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