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

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

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)123-131
Number of pages9
JournalG3: Genes, Genomes, Genetics
Volume5
Issue number1
DOIs
StatePublished - Jan 1 2015

Fingerprint

Chlorophyll
Soybeans
Chromosomes, Human, Pair 13
Exons
Mutation
Amino Acids
Genes
Phenotype
Chromosomes, Human, Pair 15
Sequence Alignment
Base Pairing
Organism Cloning
Proteins
Nucleotides
Clone Cells
Alleles
magnesium chelatase

Keywords

  • Chlorophyll
  • Duplication
  • Paralog
  • Photosynthesis
  • Soybean

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Genetics(clinical)

Cite this

Identical substitutions in nagnesium chelatase paralogs result in chlorophyll-deficient soybean mutants. / Campbell, Benjamin W.; Mani, Dhananjay; Curtin, Shaun J.; Slattery, Rebecca A.; Michno, Jean Michel; Ort, Donald Richard; Schaus, Philip J.; Palmer, Reid G.; Orf, James H.; Stupar, Robert M.

In: G3: Genes, Genomes, Genetics, Vol. 5, No. 1, 01.01.2015, p. 123-131.

Research output: Contribution to journalArticle

Campbell, BW, Mani, D, Curtin, SJ, Slattery, RA, Michno, JM, Ort, DR, Schaus, PJ, Palmer, RG, Orf, JH & Stupar, RM 2015, 'Identical substitutions in nagnesium chelatase paralogs result in chlorophyll-deficient soybean mutants', G3: Genes, Genomes, Genetics, vol. 5, no. 1, pp. 123-131. https://doi.org/10.1534/g3.114.015255
Campbell, Benjamin W. ; Mani, Dhananjay ; Curtin, Shaun J. ; Slattery, Rebecca A. ; Michno, Jean Michel ; Ort, Donald Richard ; Schaus, Philip J. ; Palmer, Reid G. ; Orf, James H. ; Stupar, Robert M. / Identical substitutions in nagnesium chelatase paralogs result in chlorophyll-deficient soybean mutants. In: G3: Genes, Genomes, Genetics. 2015 ; Vol. 5, No. 1. pp. 123-131.
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abstract = "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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AU - Michno, Jean Michel

AU - Ort, Donald Richard

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AB - 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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