Molecular Distinction between Alternative Oxidase from Monocots and Dicots

Considine, Michael J.; Holtzapffel, Ruth; Day, David A.; Whelan, James; Millar, A. Harvey

doi:10.1104/pp.004150

Cited by 181 publications

(169 citation statements)

References 40 publications

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“…The maize gene names are consistent with the standard maize nomenclature. Alternative names for the maize aox genes (according to the suggestion of Considine et al, 2002) are shown in parentheses. The number of differences per 100 amino acid residues is derived from the CLUSTAL V alignment.…”

Section: Analysis Of Aox Expression In Maize Cms Mutantsmentioning

confidence: 99%

Differential Expression of Alternative Oxidase Genes in Maize Mitochondrial Mutants

et al. 2002

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We have examined the expression of three alternative oxidase ( aox ) genes in two types of maize mitochondrial mutants. Nonchromosomal stripe (NCS) mutants carry mitochondrial DNA deletions that affect subunits of respiratory complexes and show constitutively defective growth. Cytoplasmic male-sterile (CMS) mutants have mitochondrial DNA rearrangements, but they are impaired for mitochondrial function only during anther development. In contrast to normal plants, which have very low levels of AOX, NCS mutants exhibit high expression of aox genes in all nonphotosynthetic tissues tested. The expression pattern is specific for each type of mitochondrial lesion: the NADH dehydrogenase-defective NCS2 mutant has high expression of aox2 , whereas the cytochrome oxidase-defective NCS6 mutant predominantly expresses aox3 . Similarly, aox2 and aox3 can be induced differentially in normal maize seedlings by specific inhibitors of these two respiratory complexes. Translation-defective NCS4 plants show induction of both aox2 and aox3 . AOX2 and AOX3 proteins differ in their ability to be regulated by reversible dimerization. CMS mutants show relatively high levels of aox2 mRNAs in young tassels but none in ear shoots. Significant expression of aox1 is detected only in NCS and CMS tassels. The induction pattern of maize aox genes could serve as a selective marker for diverse mitochondrial defects.

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Section: Analysis Of Aox Expression In Maize Cms Mutantsmentioning

confidence: 99%

Differential Expression of Alternative Oxidase Genes in Maize Mitochondrial Mutants

et al. 2002

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“…Increasing evidence of important differences between monocot and dicot plant lineages at a molecular level have been reported (Qiu et al, 1999;Soltis et al, 1999;Daly et al, 2001). Differences in mitochon-drial molecular function between monocots and dicots also have been highlighted recently (Fey and MarechalDrouard, 1999;Thelen et al, 1999;Considine et al, 2002). Thus, we consider it important to consider the mitochondrial proteome in a model monocot species.…”

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Towards an Analysis of the Rice Mitochondrial Proteome

et al. 2003

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Purified rice (Oryza sativa) mitochondrial proteins have been arrayed by isoelectric focusing/polyacrylamide gel electrophoresis (PAGE), by blue-native (BN) PAGE, and by reverse-phase high-performance liquid chromatography (LC) separation (LC-mass spectrometry [MS]). From these protein arrays, we have identified a range of rice mitochondrial proteins, including hydrophilic/hydrophobic proteins (grand average of hydropathicity ϭ Ϫ1.27 to ϩ0.84), highly basic and acid proteins (isoelectric point ϭ 4.0-12.5), and proteins over a large molecular mass range (6.7-252 kD), using proteomic approaches. BN PAGE provided a detailed picture of electron transport chain protein complexes. A total of 232 protein spots from isoelectric focusing/PAGE and BN PAGE separations were excised, trypsin digested, and analyzed by tandem MS (MS/MS). Using this dataset, 149 of the protein spots (the products of 91 nonredundant genes) were identified by searching translated rice open reading frames from genomic sequence and six-frame translated rice expressed sequence tags. Sequence comparison allowed us to assign functions to a subset of 85 proteins, including many of the major function categories expected for this organelle. A further six spots were matched to rice sequences for which no specific function has yet been determined. Complete digestion of mitochondrial proteins with trypsin yielded a peptide mixture that was analyzed directly by reverse-phase LC via organic solvent elution from a C-18 column (LC-MS). These data yielded 170 MS/MS spectra that matched 72 sequence entries from open reading frame and expressed sequence tag databases. Forty-five of these were obtained using LC-MS alone, whereas 28 proteins were identified by both LC-MS and gel-based separations. In total, 136 nonredundant rice proteins were identified, including a new set of 23 proteins of unknown function located in plant mitochondria. We also report the first direct identification, to our knowledge, of PPR (pentatricopeptide repeat) proteins in the plant mitochondrial proteome. This dataset provides the first extensive picture, to our knowledge, of mitochondrial functions in a model monocot plant.The ATP-synthesizing organelles of eukaryotic cells, mitochondria, can trace their origins back to an event in which one prokaryotic cell was engulfed by another cell to form a new cellular lineage containing two genomes. These genomes became dependent over time, and mitochondria lost the ability to be viable outside the host cell. A significant net transfer of genetic information occurred from the mitochondrial to the nuclear genome during this time. It is predicted that mitochondria now synthesize only a few percent of the proteins required for their function, with the majority of their proteins being encoded in the nucleus, translated in the cytosol, and transferred back to the mitochondria as protein precursors by means of targeting information in the protein sequence (Gray et al., 1999). Biochemical investigations have revealed that isolated plant mitochondria shar...

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“…Alternative oxidase expression has been studied in various organisms, but perhaps most extensively in plants where the enzyme is encoded by multigene families (Considine et al 2002). Individual genes within the family are expressed differentially in response to a variety of stresses or developmental signals (reviewed in Vanlerberghe and McIntosh 1997;ArnholdtSchmitt et al 2006;Clifton et al 2006;Rhoads et al 2006;Rhoads and Subbaiah 2007).…”

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Two Zinc-Cluster Transcription Factors Control Induction of Alternative Oxidase in Neurospora crassa

Chae

Nargang

Cleary³

et al. 2007

Genetics

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The alternative oxidase transfers electrons from ubiquinol to molecular oxygen, providing a mechanism for bypassing the later steps of the standard cytochrome-mediated electron transport chain. The enzyme is found in an array of organisms and in many cases is known to be produced in response to perturbations of the standard chain. Alternative oxidase is encoded in the nucleus but functions in the inner mitochondrial membrane. This implies the existence of a retrograde regulation pathway for communicating from the mitochondrion to the nucleus to induce alternative oxidase expression. Previous studies on alternative oxidase in fungi and plants have shown that a number of genes are required for expression of the enzyme, but the identity of these genes has remained elusive. By gene rescue we have now shown that the aod-2 and aod-5 genes of Neurospora crassa encode transcription factors of the zinc-cluster family. Electrophoretic mobility shift assays show that the DNA-binding domains of the AOD2 and AOD5 proteins act in tandem to bind a sequence element in the alternative oxidase gene promoter that is required for expression. Both proteins contain potential PAS domains near their C terminus, which are found primarily in proteins involved in signal transduction.

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Molecular Distinction between Alternative Oxidase from Monocots and Dicots

Cited by 181 publications

References 40 publications

Differential Expression of Alternative Oxidase Genes in Maize Mitochondrial Mutants

Differential Expression of Alternative Oxidase Genes in Maize Mitochondrial Mutants

Towards an Analysis of the Rice Mitochondrial Proteome

Two Zinc-Cluster Transcription Factors Control Induction of Alternative Oxidase in Neurospora crassa

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