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2015, DOI: 10.1534/g3.114.015255

Identical substitutions in magnesium chelatase paralogs result in chlorophyll-deficient soybean mutants


Benjamin W. Campbell, Dhananjay Mani, Shaun J. Curtin, Rebecca A. Slattery, Jean-Michel Michno, Donald R. Ort, Philip J. Schaus, Reid G. Palmer, James H. Orf, and Robert M. Stupar


The soybean [Glycine max (L.) Merr.] chlorophyll-deficient line MinnGold is a spontaneous mutant characterized by yellow foliage. Map-based cloning and transgenic complementation revealed that the mutant phenotype is caused by a nonsynonymous nucleotide substitution in the third exon of a Mg-chelatase subunit gene (ChlI1a) on chromosome 13. This gene was selected as a candidate for a different yellow foliage mutant, T219H (Y11y11), that had been previously mapped to chromosome 13. Although the phenotypes of MinnGold and T219H are clearly distinct, sequencing of ChlI1a in T219H identified a different nonsynonymous mutation in the third exon, only six base pairs from the MinnGold mutation. This information, along with previously published allelic tests, were used to identify and clone a third yellow foliage mutation, CD-5, which was previously mapped to chromosome 15. This mutation was identified in the ChlI1b gene, a paralog of ChlI1a. Sequencing of the ChlI1b allele in CD-5 identified a nonsynonymous substitution in the third exon that confers an identical amino acid change as the T219H substitution at ChlI1a. Protein sequence alignments of the two Mg-chelatase subunits indicated that the sites of amino acid modification in MinnGold, T219H, and CD-5 are highly conserved among photosynthetic species. These results suggest that amino acid alterations in this critical domain may create competitive inhibitory interactions between the mutant and wild-type ChlI1a and ChlI1b proteins.

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The Ort Lab is supported by many public and private partnerships, including the Bill & Melinda Gates Foundation, the Foundation for Food and Agriculture Research, the UK Government's Department for International Development, the U.S. Department of Energy, and the Advanced Research Projects Agency-Energy.

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