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Papers In Press, published online ahead of print August 23, 2000
J. Biol. Chem, 10.1074/jbc.M005699200
Submitted on June 28, 2000
Accepted on August 23, 2000
and 
Tubulins of Antarctic Fishes
Biology, Northeastern University, Boston, MA 02115
Corresponding Author: iceman{at}neu.edu
The microtubules of Antarctic fishes assemble at very low temperatures (-1.8 oC). The adaptations that enhance assembly of these microtubules are intrinsic to the tubulin dimer and reduce its critical concentration for polymerization at 0 oC to 0.9 mg/ml [Williams, R. C., Jr., Correia, J. J., and DeVries, A. L. (1985) Biochemistry 24, 2790-2798]. Here we demonstrate that microtubules formed by pure brain tubulins of Antarctic fishes exhibit slow dynamics at both low (5 oC) and high (25 oC) temperatures: rates of polymer growth and shortening, and the frequencies of interconversion between these states, are small relative to those observed for mammalian microtubules (37 oC). To investigate the contribution of tubulin primary sequence variation to the functional properties of the microtubules of Antarctic fishes, we have sequenced brain cDNAs that encode 9 
and 4 
tubulins from the rockcod Notothenia coriiceps and 4 and 2 tubulins from the icefish Chionodraco rastrospinosus. The tubulins of these fishes were found to contain small sets of unique or rare residue substitutions that map to the lateral, interprotofilament surfaces or to the interiors of the and polypeptides; longitudinal interaction surfaces are not altered in the fish tubulins. Four changes (A278T and S287T in ; S280G and A285S in ) were present in the S7-H9 interprotofilament "M" loops of some monomers and would be expected to increase the flexibility of these regions. A fifth lateral substitution specific to the chain (M302L,F) may increase the hydrophobicity of the interprotofilament interaction. Two hydrophobic substitutions (:S187A in helix H5, :Y202F in sheet S6) may stabilize the monomers in conformations favorable to polymerization. We propose that cold adaptation of microtubule assembly in Antarctic fishes has occurred in part by evolutionary restructuring of the lateral surfaces and the cores of the tubulin monomers.
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