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Cloning and characterization of Arenicola marina peroxiredoxin 6, an annelid two-cysteine peroxiredoxin highly homologous to mammalian one-cysteine peroxiredoxins
Loumaye, E.; Andersen, A.C.; Clippe, A.; Degand, H.; Dubuisson, M.; Zal, F.; Morsomme, P.; Rees, J.F.; Knoops, B. (2008). Cloning and characterization of Arenicola marina peroxiredoxin 6, an annelid two-cysteine peroxiredoxin highly homologous to mammalian one-cysteine peroxiredoxins. Free Radic. Biol. Med. 45(4): 482-493. http://dx.doi.org/10.1016/j.freeradbiomed.2008.04.033
In: Free Radical Biology and Medicine. Elsevier: New York; Oxford. ISSN 0891-5849; e-ISSN 1873-4596
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoorden
    Annelida [WoRMS]; Arenicola marina (Linnaeus, 1758) [WoRMS]
    Marien/Kust
Author keywords
    Annelid; Arenicola marina; Peroxidase; Peroxiredoxin; Antioxidant
Auteurs  Top 
  • Loumaye, E.
  • Andersen, A.C.
  • Clippe, A.
  • Degand, H.
  • Dubuisson, M.
  • Zal, F.
  • Morsomme, P.
  • Rees, J.F.
  • Knoops, B.
Abstract
    Peroxiredoxins (PRDXs) are a superfamily of thiol-dependent peroxidases found in all phyla. PRDXs are mechanistically divided into three subfamilies, namely typical 2-Cys, atypical 2-Cys, and 1-Cys PRDXs. To reduce peroxides, the N-terminal peroxidatic Cys of PRDXs is first oxidized into sulfenic acid. This intermediate is reduced by forming a disulfide bond either with a resolving Cys of another monomeric entity (typical 2-Cys) or of the same molecule (atypical 2-Cys). In 1-Cys PRDXs, the resolving Cys is missing and the sulfenic acid of the peroxidatic Cys is reduced by a heterologous thiol-containing reductant. In search of a homolog of human 1-Cys PRDX6 in Arenicola marina, an annelid worm living in intertidal sediments, we have cloned and characterized a PRDX exhibiting high sequence homology with its mammalian counterpart. However, A. marina PRDX6 possesses five Cys among which two Cys function as peroxidatic and resolving Cys of typical 2-Cys PRDXs. Thus, A. marina PRDX6 belongs to a transient group exhibiting sequence homologies with mammalian 1-Cys PRDX6 but must be mechanistically classified into typical 2-Cys PRDXs. Moreover, PRDX6 is highly expressed in tissues directly exposed to the external environment, suggesting that this PRDX may be of particular importance for protection against exogenous oxidative attacks.
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