Betaine Deficiency in Maize

Lerma, Claudia; Rich, Patrick J.; Ju, G; Yang, Wen-Ju; Hanson, Andrew D.; Rhodes, David

doi:10.1104/pp.95.4.1113

Cited by 41 publications

(32 citation statements)

References 19 publications

(36 reference statements)

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“…The levels of free Cho accumulated by PEAMT ϩ transgenics are well above normal ranges for plant tissues, where the ceiling is Ϸ1 mol g Ϫ1 FW (25)(26)(27). However, these free Cho levels are below those that can accumulate in plant tissues supplied with Cho, as are the phosphocholine levels (15,28).…”

Section: Peamt Overexpression Depletes Ea and Phosphoethanolamine Poolsmentioning

confidence: 99%

Enhanced synthesis of choline and glycine betaine in transgenic tobacco plants that overexpress phosphoethanolamine N -methyltransferase

McNeil

Nuccio

Ziemak

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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176

132

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Choline (Cho) is the precursor of the osmoprotectant glycine betaine and is itself an essential nutrient for humans. Metabolic engineering of Cho biosynthesis in plants could therefore enhance both their resistance to osmotic stresses (drought and salinity) and their nutritional value. The key enzyme of the plant Cho-synthesis pathway is phosphoethanolamine N-methyltransferase, which catalyzes all three of the methylations required to convert phosphoethanolamine to phosphocholine. We show here that overexpressing this enzyme in transgenic tobacco increased the levels of phosphocholine by 5-fold and free Cho by 50-fold without affecting phosphatidylcholine content or growth. Moreover, the expanded Cho pool led to a 30-fold increase in synthesis of glycine betaine via an engineered glycine betaine pathway. Supplying the transgenics with the Cho precursor ethanolamine (EA) further enhanced Cho levels even though the supplied EA was extensively catabolized. These latter results establish that there is further scope for improving Cho synthesis by engineering an increased endogenous supply of EA and suggest that this could be achieved by enhancing EA synthesis and͞or by suppressing its degradation.

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Section: Peamt Overexpression Depletes Ea and Phosphoethanolamine Poolsmentioning

confidence: 99%

Enhanced synthesis of choline and glycine betaine in transgenic tobacco plants that overexpress phosphoethanolamine N -methyltransferase

McNeil

Nuccio

Ziemak

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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176

132

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“…Therefore, the inability of rice plants to accumulate glycinebetaine can be probably ascribed in part to a deficiency in the choline oxidation step. The CMO gene in the rice g e n o m e might be either absent or silent (as in maize glycinebetaine deficient lines (Lerma et al, 1991)). If this is the case, then introduction of the CMO gene into rice plants m a y enable t h e m to accumulate glycinebetaine and i m p r o v e salt tolerance.…”

Section: Resultsmentioning

confidence: 99%

“…In others (barley, wheat, rye and certain maize varieties), it runs up to about 10 limol/g fresh weight (Hanson, 1980;Ishitani et aL, 1993;Lerma et aL, 1991;Rathinasabapathi etaL, 1993). Rice is especially salt-sensitive, mainly at the stage of young seedlings (Flowers and Yeo, 1981).…”

Section: Introductionmentioning

confidence: 99%

Expression of a betaine aldehyde dehydrogenase gene in rice, a glycinebetaine nonaccumulator, and possible localization of its protein in peroxisomes

Yokota²,

et al. 1997

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SummaryBetaine aldehyde dehydrogenase (BADH) catalyzes the last step in the plant biosynthetic pathway that leads to glycinebetaine. Rice plants (Oryza sativa L.}, albeit considered a typical non-glycinebetaine accumulating species, have been found to express this enzyme at low levels. This observation evokes an interest in phylogenic evolution of the enzyme in the plant kingdom. It is reported here that rice plants possess the ability to take up exogenously added betaine aldehyde through the roots and convert it to glycinebetaine, resulting in an enhanced salttolerance of the plants. A gene encoding a putative BADH from the rice genome was also cloned and sequenced. The gene was found to contain 14 introns, and the overall nucleotide sequence of the coding region is c. 78% identical to that of the barley BADH cDNA. Cloning of a partial BADH cDNA from rice was accomplished by reverse transcription-polymerase chain reaction (RT-PCR). The nucleotide sequence of the cloned fragment was found to be identical to the corresponding exon regions of the rice genomic BADH gene. The deduced amino acid sequences of rice and barley BADH both contain a C-terminal tripeptide SKL, a signal known to target preproteins to microbodies. This localization was confirmed by an immuno-gold labeling study of transgenic tobacco harboring barley cDNA, which showed BADH protein inside peroxisomes. Northern blot analysis revealed that the level of BADH mRNA is salt-inducible.

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“…Overexpression of BADH results in increase of tolerance of salt and osmotic stresses in many organisms [21][22][23]. Using Agrobacterium tumefaciens strain LBA4404 carrying a binary vector pBin438 and a leaf regeneration system, Jia et al [20] demonstrated that overexpression of the BADH gene cloned from Atriplex hortensis in a salt-sensitive to *Address correspondence to these authors at the Institute of Turfgrass Science, Beijing Forestry University, Beijing 100083, China; Tel: 010-919-684-6507; Fax: 010-919-668-0795; E-mail: hanliebao@163.com Institute for Genome Sciences and Policy, Duke University, Durham 27708, USA; Tel: +86-10-6233-7982; Fax: +86-10-6232-2089; E-mail: wei.tang@duke.edu mato cultivar, Bailichun, improved salt tolerance.…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of the Betaine Aldehyde Dehydrogenase Gene in

Li¹,

Zeng²,

Xue³

et al. 2010

TOBIOTJ

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Betaine aldehyde dehydrogenase (BADH) catalyzes the last step in the synthesis of the glycine betaine from choline. The BADH gene from turfgrass Ophiopogon japonicus has not been reported. In this study, we first isolated the full length cDNA of betaine aldehyde dehydrogenase gene (OjBADH) from O. japonicus using Reverse TranscriptasePolymerase Chain Reaction (RT-PCR) and Rapid Amplification of cDNA Ends (RACE) techniques. The OjBADH gene (GenBank accession number: DQ645888) has 1785 nucleotides with the 5' untranscribed region (UTR) of 63 nucleotides, 3' UTR of 219 nucleotides, and an open reading frame of 1503 nucleotides. This gene encodes a polypeptide of 500 amino acids. It shares a high homology with BADH genes of other Chenopodiaceae species. The putative protein includes a conservative region of phosphofructokinase, aldehyde dehydrogenase, and glutamy phosphoric acid reductase. Overexpression of OjBADH in transgenic tobacco plants demonstrated 2-2.5 folds increase of glycine betaine content and 60-85% increase of survival rate under salt tolerance. These results suggested that the O. japonicus BADH gene may be used to engineer plants for salt stress tolerance.

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Betaine Deficiency in Maize

Cited by 41 publications

References 19 publications

Enhanced synthesis of choline and glycine betaine in transgenic tobacco plants that overexpress phosphoethanolamine N -methyltransferase

Enhanced synthesis of choline and glycine betaine in transgenic tobacco plants that overexpress phosphoethanolamine N -methyltransferase

Expression of a betaine aldehyde dehydrogenase gene in rice, a glycinebetaine nonaccumulator, and possible localization of its protein in peroxisomes

Isolation and Characterization of the Betaine Aldehyde Dehydrogenase Gene in

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