The maize Oil Yellow1 (Oy1) gene encodes the I subunit of magnesium chelatase

Ruairidh Sawers, Joanne Viney, Phyllis R. Farmer, Rhiannon R. Bussey, Gregory Olsefski, Katya Anufrikova, C. Neil Hunter, Thomas P. Brutnell

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

Semi-dominant Oil yellow1 (Oy1) mutants of maize (Zea mays) are deficient in the conversion of protoporphyrin IX to magnesium protoporphyrin IX, the first committed step of chlorophyll biosynthesis. Using a candidate gene approach, a cDNA clone was isolated that was predicted to encode the I subunit of magnesium chelatase (ZmCHLI) and mapped to the same genetic interval as Oy1. Allelic variation was identified at ZmCHLI between wild-type plants and plants carrying semi-dominant alleles of Oy1. These differences revealed putative amino acid substitutions that could account for the alterations in protein function. Candidate lesions were tested by introduction of homologous changes into the Synechocystis magnesium chelatase I gene (SschlI) and characterization of the activity of mutant protein variants in an in vitro enzyme activity assay. The results of these analyses suggest that SsChlI protein variants containing the substitutions identified in the dominant Oy1 maize alleles lack activity necessary for magnesium chelation and confer a semi-dominant phenotype via competitive inhibition of wild-type SsChlI.

Original languageEnglish (US)
Pages (from-to)95-106
Number of pages12
JournalPlant molecular biology
Volume60
Issue number1
DOIs
StatePublished - Jan 1 2006

Fingerprint

magnesium chelatase
Corn Oil
corn oil
Oils
oils
Zea mays
Alleles
Genes
alleles
Synechocystis
mutants
protoporphyrin
lesions (plant)
genes
chelation
proteins
Enzyme Assays
amino acid substitution
Mutant Proteins
Amino Acid Substitution

All Science Journal Classification (ASJC) codes

  • Agronomy and Crop Science
  • Genetics
  • Plant Science

Cite this

Sawers, R., Viney, J., Farmer, P. R., Bussey, R. R., Olsefski, G., Anufrikova, K., ... Brutnell, T. P. (2006). The maize Oil Yellow1 (Oy1) gene encodes the I subunit of magnesium chelatase. Plant molecular biology, 60(1), 95-106. https://doi.org/10.1007/s11103-005-2880-0
Sawers, Ruairidh ; Viney, Joanne ; Farmer, Phyllis R. ; Bussey, Rhiannon R. ; Olsefski, Gregory ; Anufrikova, Katya ; Hunter, C. Neil ; Brutnell, Thomas P. / The maize Oil Yellow1 (Oy1) gene encodes the I subunit of magnesium chelatase. In: Plant molecular biology. 2006 ; Vol. 60, No. 1. pp. 95-106.
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Sawers, R, Viney, J, Farmer, PR, Bussey, RR, Olsefski, G, Anufrikova, K, Hunter, CN & Brutnell, TP 2006, 'The maize Oil Yellow1 (Oy1) gene encodes the I subunit of magnesium chelatase', Plant molecular biology, vol. 60, no. 1, pp. 95-106. https://doi.org/10.1007/s11103-005-2880-0

The maize Oil Yellow1 (Oy1) gene encodes the I subunit of magnesium chelatase. / Sawers, Ruairidh; Viney, Joanne; Farmer, Phyllis R.; Bussey, Rhiannon R.; Olsefski, Gregory; Anufrikova, Katya; Hunter, C. Neil; Brutnell, Thomas P.

In: Plant molecular biology, Vol. 60, No. 1, 01.01.2006, p. 95-106.

Research output: Contribution to journalArticle

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AU - Sawers, Ruairidh

AU - Viney, Joanne

AU - Farmer, Phyllis R.

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AU - Olsefski, Gregory

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AU - Hunter, C. Neil

AU - Brutnell, Thomas P.

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N2 - Semi-dominant Oil yellow1 (Oy1) mutants of maize (Zea mays) are deficient in the conversion of protoporphyrin IX to magnesium protoporphyrin IX, the first committed step of chlorophyll biosynthesis. Using a candidate gene approach, a cDNA clone was isolated that was predicted to encode the I subunit of magnesium chelatase (ZmCHLI) and mapped to the same genetic interval as Oy1. Allelic variation was identified at ZmCHLI between wild-type plants and plants carrying semi-dominant alleles of Oy1. These differences revealed putative amino acid substitutions that could account for the alterations in protein function. Candidate lesions were tested by introduction of homologous changes into the Synechocystis magnesium chelatase I gene (SschlI) and characterization of the activity of mutant protein variants in an in vitro enzyme activity assay. The results of these analyses suggest that SsChlI protein variants containing the substitutions identified in the dominant Oy1 maize alleles lack activity necessary for magnesium chelation and confer a semi-dominant phenotype via competitive inhibition of wild-type SsChlI.

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