Abstract
A nodulin gene coding for a polypeptide with an apparent M(r) of 24,000 (nodulin-24) was isolated from soybean (Glycine max). DNA sequence analysis of this gene revealed that its coding capacity is for a polypeptide of only M(r) 15,100 and is interrupted by four introns. The three middle exons and their flanking segments appear to have been generated by duplications of a unit resembling an insertion sequence. This unit is bounded by a 12-base-pair inverted repeat and encompasses the 54-base-pair exon corresponding to each of three central hydrophobic domains of the protein, nodulin-24. The resulting repeated hydrophobic structure of this protein may be responsible for an apparent increase in M(r) from 15,100 to 24,000. In vitro translation and immunological studies suggest that nodulin-24 is a precursor and is processed cotranslationally into a M(r) 20,000 polypeptide. This polypeptide is a component of the membrane envelope enclosing the bacteroids (peribacteroid membrane) synthesized during symbiosis with Rhizobium. The low degree (<6%) of sequence divergence among the repeated units suggests that this gene has been generated recently during the evolution of symbiotic nitrogen fixation in soybean.