Biology Reference
In-Depth Information
Ph -2/2HbO displays unique adaptive structural properties ensuring higher
flexibility, thus facilitating its function at low temperatures, for example, by
enhancing the capacity for correct positioning of ligand(s), which would be
made more difficult by a rigid structure. In summary, this globin is a notable
case study of relationship between molecular structure, cold adaptation and a
wide range of equally important biological functions.
Hexacoordinated globins in Antarctic microorganisms call for efforts in
shedding light on their place and role in the context of evolution. Knowl-
edge of the range of their functions and physiological role in vivo is still
incomplete and a matter of lively debate. However, modern concepts of
biological sciences appear more and more to support the idea that the phys-
iological role of a given molecule is not restricted to a single aspect, although
one aspect may well be predominant. Based on this assumption, the current
knowledge summarised in this review seems to be a useful starting point to
achieve progress by further investigations aimed at increasing our albeit
incomplete understanding of the biological function of a fundamentally
important class of macromolecules such as globins, not only Ph -2/
2HbO—a valuable case study—but also other globins, for example, Ngb
and Cygb, whose biomedical significance is steadily growing.
ACKNOWLEDGEMENTS
The authors wish to thank the Centre de Ressources Biologiques de l'Institut Pasteur, Paris,
France ( http://www.crbip.pasteur.fr ) for supplying the P. haloplanktis CIP 108707 strain.
This study was carried out in the framework of the SCAR programme “Antarctic
Thresholds-Ecosystem Resilience and Adaptation” (AnT-ERA), and of the “Coordination
Action for Research Activities on Life in Extreme Environments” (CAREX), European
Commission FP7 call ENV.2007.2.2.1.6. It was financially supported by the Italian
National Programme for Antarctic Research (PNRA).
F. M. is supported by a fellowship from the Australian Research Council (DE120102610).
M. T.-T. is supported by Consejo Nacional de Ciencia y Tecnologia (CONACyT)
(Mexico) through grant number 99171 and Consejo Estatal de Ciencia, Tecnolog´ae
Innovaci´n de Michoac´n (CECTI) through grant number 007. Thanks are due to Prof.
Robert K. Poole for kindly inviting us to submit this review. We apologise in case we
have neglected references relevant to the subject.
REFERENCES
Abell, G. C., & Bowman, J. P. (2005). Ecological and biogeographic relationships of class
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Abergel, C., Walburger, A., Chenivesse, S., & Lazdunski, C. (2001). Crystallization and pre-
liminary crystallographic study of the peptidoglycan-associated lipoprotein from
Escherichia coli . Acta Crystallographica. Section D, Biological Crystallography , 57 , 317-319.
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