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Nucleic Acids Research, 1987, Vol. 15, No. 3 1271-1280
© 1987

Articles

Several nodulins of soybean share structural domains but differ in their subcellular locations

Fred A. Jacobs1, Mingda Zhang, Marc G. Fortin and Desh Pal S. Verma*

Centre for Plant Molecular Biology, Department of Biology, McGill University Montreal, H3A 1B1, Canada

*To whom correspondence should be addressed

Received August 21, 1986. Revised December 11, 1986. Accepted December 11, 1986.

Four soybean cDNA nodule-specific clones encoding nodulin-23, -26b, -27 and -44 were observed to cross-hybridize under low stringency conditions. Nucleotide sequence analysis revealed that the cDNAs contain three distinct domains: two domains with 70 to 95% homology separated by a third domain unique to each cDNA. Despite a number of nucleotide insertions and deletions, the protein sequences are conserved in the two domains which correlate with the homologous nucleotide domains. The amino terminal domain of each nodulin contains putative signal sequences for membrane translocation, although only two (nodulin-23 and -44) meet all the criteria for a functional signal. Immuno-precipitation of hybrid-release translation products of the four cDNAs revealed that nodulin-23 is associated with the peribacteroid membrane while nodulin-27 is in the cytoplasmic fraction of the nodule. These four nodulins are members of a diverse family with conserved structural features and the genes encoding them appear to have recently evolved from a common ancestor.

1Current address: Biotechnology Research Institute, Montreal, Canada


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