Globin-like proteins in Caenorhabditis elegans: in vivo localization, ligand binding and structural properties. - Inserm - Institut national de la santé et de la recherche médicale Access content directly
Journal Articles BMC Biochemistry Year : 2010

Globin-like proteins in Caenorhabditis elegans: in vivo localization, ligand binding and structural properties.

Eva Geuens
  • Function : Author
  • PersonId : 908146
Evi Vinck
  • Function : Author
  • PersonId : 908149
Alessandra Pesce
  • Function : Author
  • PersonId : 908150
Angela Fago
  • Function : Author
  • PersonId : 908152
Lesley Tilleman
  • Function : Author
  • PersonId : 908153
Sasha de Henau
  • Function : Author
  • PersonId : 908154
Roy Weber
  • Function : Author
  • PersonId : 908156
Sabine van Doorslaer
  • Function : Author
  • PersonId : 875893
Jacques Vanfleteren
  • Function : Author
  • PersonId : 908157
Luc Moens
  • Function : Author
  • PersonId : 875896


BACKGROUND: The genome of the nematode Caenorhabditis elegans contains more than 30 putative globin genes that all are transcribed. Although their translated amino acid sequences fit the globin fold, a variety of amino-acid substitutions and extensions generate a wide structural diversity among the putative globins. No information is available on the physicochemical properties and the in vivo expression. RESULTS: We expressed the globins in a bacterial system, characterized the purified proteins by optical and resonance Raman spectroscopy, measured the kinetics and equilibria of O2 binding and determined the crystal structure of GLB-1* (CysGH2 --> Ser mutant). Furthermore, we studied the expression patterns of glb-1 (ZK637.13) and glb-26 (T22C1.2) in the worms using green fluorescent protein technology and measured alterations of their transcript abundances under hypoxic conditions.GLB-1* displays the classical three-over-three alpha-helical sandwich of vertebrate globins, assembled in a homodimer associated through facing E- and F-helices. Within the heme pocket the dioxygen molecule is stabilized by a hydrogen bonded network including TyrB10 and GlnE7.GLB-1 exhibits high ligand affinity, which is, however, lower than in other globins with the same distal TyrB10-GlnE7 amino-acid pair. In the absence of external ligands, the heme ferrous iron of GLB-26 is strongly hexacoordinated with HisE7, which could explain its extremely low affinity for CO. This globin oxidizes instantly to the ferric form in the presence of oxygen and is therefore incapable of reversible oxygen binding. CONCLUSION: The presented data indicate that GLB-1 and GLB-26 belong to two functionally-different globin classes.
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Dates and versions

inserm-00615497 , version 1 (19-08-2011)



Eva Geuens, David Hoogewijs, Marco Nardini, Evi Vinck, Alessandra Pesce, et al.. Globin-like proteins in Caenorhabditis elegans: in vivo localization, ligand binding and structural properties.. BMC Biochemistry, 2010, 11 (1), pp.17. ⟨10.1186/1471-2091-11-17⟩. ⟨inserm-00615497⟩
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