TY - JOUR
T1 - Comparative structure and chemistry of tubulins from different eukaryotes
AU - Luduena, Richard F.
AU - Little, Melvyn
N1 - Funding Information:
Supported by a Robert Welch Foundation grant (AQ-726) to R.F. Luduena and a NATO Travel Fellowship to M. Little.
PY - 1981
Y1 - 1981
N2 - Electrophoretic and peptide mapping have been used to examine α- and β-tubulins from chordates, tunicates, echinoderms, mollusks, brachiopods, ferns, fungi, green algae and heliozoans. Cytoplasmic, ciliary, flagellar, and axopodial tubulins were examined. The results show that β-tubulin is more conserved than α-tubulin. The large differences seen between axonemal and cytoplasmic tubulins and the similarity of all axonemal tubulins examined indicate that the genes for these two tubulin classes diverged prior to the appearance of metazoa and metaphyta. Comparisons of α-tubulins appear useful for tracing phyletic relationships within kingdoms whereas comparisons of β-tubulins may be better for relating the kingdoms to each other.
AB - Electrophoretic and peptide mapping have been used to examine α- and β-tubulins from chordates, tunicates, echinoderms, mollusks, brachiopods, ferns, fungi, green algae and heliozoans. Cytoplasmic, ciliary, flagellar, and axopodial tubulins were examined. The results show that β-tubulin is more conserved than α-tubulin. The large differences seen between axonemal and cytoplasmic tubulins and the similarity of all axonemal tubulins examined indicate that the genes for these two tubulin classes diverged prior to the appearance of metazoa and metaphyta. Comparisons of α-tubulins appear useful for tracing phyletic relationships within kingdoms whereas comparisons of β-tubulins may be better for relating the kingdoms to each other.
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U2 - 10.1016/0303-2647(81)90030-7
DO - 10.1016/0303-2647(81)90030-7
M3 - Article
C2 - 7337806
AN - SCOPUS:0019762345
SN - 0303-2647
VL - 14
SP - 231
EP - 238
JO - Currents in modern biology
JF - Currents in modern biology
IS - 3-4
ER -