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J. Biol. Chem., Vol. 275, Issue 47, 37038-37047, November 24, 2000
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- AND 
-TUBULINS OF ANTARCTIC FISHES*
§,,
, and
From the The microtubules of Antarctic fishes,
unlike those of homeotherms, assemble at very low temperatures
( Department of Biology, Northeastern
University, Boston, Massachusetts 02115, the ¶ Department of
Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235, and the Life Science Division, Lawrence Berkeley National
Laboratory, Berkeley, California 94720
1.8 °C). The adaptations that enhance assembly of these
microtubules are intrinsic to the tubulin dimer and reduce its critical
concentration for polymerization at 0 °C 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 °C) and high (25 °C) temperatures; the rates of polymer growth and shortening and the frequencies of
interconversion between these states are small relative to those
observed for mammalian microtubules (37 °C). 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 -tubulins and 4 -tubulins from the
yellowbelly rockcod Notothenia coriiceps and 4 -tubulins and 2 -tubulins from the ocellated icefish Chionodraco
rastrospinosus. The tubulins of these fishes were found to
contain small sets of unique or rare residue substitutions that mapped
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 or M302F) may increase the hydrophobicity
of the interprotofilament interaction. Two hydrophobic substitutions (:S187A in helix H5 and :Y202F in sheet S6) may act to 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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