Two alloplasmic wheat lines having the same common wheat nucleus but the cytoplasms of
Aegilops crassa and
Ae. columnaris together with the corresponding normal line (control) were used in the two-dimensional gel electrophoresis of soluble and thylakoid membrane proteins of the chloroplast. Three chloroplast polypeptides: the Rubisco large subunit, the β subunit of ATP synthase, and an unidentified 31 kDa protein, differed in the common wheat and two
Aegilops cytoplasms. Three chloroplast genes,
atpB,
atpE and
trnM, that respectively encode the β and ε subunits of ATP synthase and tRNA
met, were sequenced. The
atpB gene differed by two synonymous base substitutions, whereas the other two genes were identical in the two
Aegilops cytoplasms. From the predicted amino acid sequences, the β subunits of the ATP synthase in the
Aegilops cytoplasms were assumed to have three amino acid substitutions: Ala by Val, Asp
- by Ala, and Gin by Lys
+, in contrast to the cytoplasm of common wheat. This accounts for the difference in pI values found for the common wheat and
Aegilops cytoplasms. The two base substitutions for the
atpE genes of common wheat and the
Aegilops cytoplasms were synonymous. The differences detected in the genes encoding the two subunits of ATP synthase do not appear to be ascribable to the differences in phenotypic effects for the common wheat and
Aegilops cytoplasms. The base substitution rate of the
atpB-atpE-trnM gene cluster was similar to that of the
rbcL gene. From the rate for the
atpB gene alone, evolutionary divergence of the wheat-
Aegilops complex is assumed to have begun ca. 3.0×10
6 years ago, as compared to ca. 8.0×10
6 years ago for the divergence of the wheat-
Aegilops complex and barley.
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