Structural Characterization of Piscine Globin Superfamily Proteins

Globin superfamily proteins including myoglobin and hemoglobin, have welcome new members recently, namely, cytoglobin, neuroglobin and globin X, though their physiological functions are still to be addressed. Fish are the excellent models for the study of these globins, but their characteristics have not yet been discussed to date. In the present study, attempts have been made to characterize their structural uniqueness by making use of proteomics approach. This is the first comparative study on the characterization of globin superfamily proteins from fish.

Authors:



References:
[1] A. Roesner, "A globin gene of ancient evolutionary origin in lower
vertebrates: Evidence for two distinct globin families in animals," Mol.
Biol. Evol., vol. 22, 12-20, 2005
[2] T. Burmester, B. Weich, S. Reinhardt, and T. Hankeln, "A vertebrate
globin expressed in the brain," Nature, vol.407, 520-523, 2000
[3] T. Burmester, B. Ebner, B. Weich, and T. Hankeln, "Cytoglobin: a novel
globin type ubiquitously expressed in vertebrate tissues," Mol. Biol. Evol.,
vol. 19, 416-421, 2002.
[4] D. Kugelstadt, M. Haberkamp, T. Hankeln, and T. Burmester,
"Neuroglobin, cytoglobin, and a novel, eye-specific globin from
chicken," Biochem. Biophys. Res. Commun., vol. 325, 719-725, 2004.
[5] C. Fuchs, T. Burmester, and T. Hankeln, "The amphibian globin gene
repertoire as revealed by the Xenopus genome," Cytogenet. Genome Res.,
112, 296-306, 2006
[6] A. Roesner, C. Fuchs, T. Hankeln, and T. Burmester, "A globin gene of
ancient evolutionary origin in lower vertebrates: evidence for two distinct
globin families in animals," Mol. Biol. Evol., vol. 22, 12-20, 2005.
[7] J. Fraser, L.V. de Mello, D. Ward, H.H. Rees, D.R. Williams, Y. Fang, A.
Brass, A.Y. Gracey, and A.R. Cossins, "Hypoxia-inducible myoglobin
expression in nonmuscle tissues," Proc. Natl. Acad. Sci. USA, vol. 103,
2977-2981, 2006.
[8] H. Wajcman, L. Kiger, and M. C. Marden, "Structure and function
evolution in the superfamily of globins," Com. Rend. Biol., vol. 332,
pp.273-282, 2009
[9] S. Dewilde, L. Kiger, T. Burmester, T. Hankein, V. Baudin-Creuza, T.
Aerts, M.C. Marden, R. Caubergs, and L. Moens, "Biochemical
characterizaition and ligand binding properties of neuroglobin, a novel
member of the globin family," J. Biol. Chem., vol. 276, 2001.
[10] Y. Enoki, K. Matsumura, Y. Ohga, H. Kohzuki, and M. Hattori, "Oxygen
affinities (p50) of myoglobins from four vertebrate species (Canis
familiaris, Rattus norvegicus, Mus musculus and Gallus domesticus) as
determined by a kinetic and an equilibrium method," Comp. Biochem.
Physiol. B, vol. 110, 193-199, 1995.
[11] R.A. Meyer, H.L. Sweeney, and M.J. Kushmerick, "A simple analysis of
the phosphocreatine shuttle," Am. J. Physiol., vol. 246, C365-C377,
1984.
[12] P.W. Hochachka, "The metabolic implications of intracellular
circulation," Proc. Natl. Acad. Sci. USA, vol. 96, 12233-12239, 1999.
[13] S.E. Flonta, S. Arena, A. Pisacane, P. Michieli, and A. Bardelli,
"Expression and functional regulation of myoglobin in epithelial
cancers," Am. J. Pathol., vol. 175:201-206, 2009.
[14] M. Brunori, "Myoglobin strikes back," Protein Sci., vol. 19, 195-201,
2010.
[15] T. Burmester and T. Hankeln, "What is the function of neuroglobin?," J.
Exp. Biol., vol. 212, 1423-1428, 2009.
[16] T.A. Hall, "BioEdit: a user-friendly biological sequence alignment editor
and analysis program for Windows 95/98/NT," Nucleic Acids Symp. Ser.
vol. 41, 95-98, 1999.
[17] K. Tamura, J. Dudley, M. Nei, and S, Kumar, "MEGA4: Molecular
Evolutionary Genetics Analysis (MEGA) software version 4.0," Mol.
Biol. Evol., vol. 24, 1596-1599, 2007.
[18] J. Kyte and R.F. Doolittle, "A simple method for displaying the
hydrophopathic character of a protein," J. Mol. Biol., vol. 157, 105-132,
1982.
[19] T. Schwede, J. Kopp, N. Guex, and M.C. Peitsch, "SWISS-MODEL: an
automated protein homology-modeling server," Nucleic Acids Res., vol.
31, 3381-3385, 2003.
[20] J.M. Stewart, J.A. Blakely, P.A. Karpowicz, E. Kalanxhi, B.J. Thatcher,
and B.M. Martin, "Unusually weak oxygen binding, physical properties,
partial sequence, autoxidation rate and a potential phosphorylation site of
beluga whale (Delphinapterus leucas) myoglobin," Comp. Biochem.
Physiol. B, vol. 137, 401-412, 2004.
[21] E.W. Grunwald and M.P. Richards, "Studies with myoglobin variants
indicate that released hemin is the primary promoter of lipid oxidation in
washed fish muscle," J. Agric. Food Chem., vol. 54, 4452-4460, 2006.
[22] W.C.B. Regis, J. Fattori, M.M. Santoro, M. Jamin, and C.H.I. Ramos,
"On the difference in stability between horse and sperm whale
myoglobins," Arch. Biochem. Biophys., 436, 168-177, 2005.
[23] Y. Ochiai, N. Ueki, and S. Watabe, "Effects of point mutations on the
structural stability of tuna myoglobins," Comp. Biochem. Physiol. B, vol.
153, 223-228, 2009.
[24] N. Ueki and Y Ochiai, "Primary structure and thermostability of bigeye
tuna myoglobin in relation to those from other scombridae fish," Fish.
Sci., vol. 70, 875-884, 2004.
[25] H.S. Ajoula, M.T. Wilson, and I.E.G. Morrison, "Functional
consequences of haem orientational disorder in sperm-whale and
yellow-fin-tuna myoglobins," Biochem. J., vol. 243, 205-210, 1987.
[26] A. Wawrowski, F. Gerlach, T. Hankein, and T. Burmester, "Changes of
globin expression in the Japanese medaka (Oryzias latipes) in response to
acute and chronic hypoxia," J. Comp. Physiol. B, vol. 188, 199-208,
2011.
[27] A.Roesner, S.A. Mitz, T. Hankeln, and T. Burmester, "Globins and
hypoxia adaptation in the goldfish, Carassius auratus," FEBS J., vol. 275,
3633-3643, 2008.