A single mutation that increases maize seed weight.

Giroux, Michael J.; Shaw, Janine R.; Barry, Gerard F.; Cobb, B. G.; Greene, Thomas W.; Okita, Thomas W.; Hannah, L. Curtis

doi:10.1073/pnas.93.12.5824

Cited by 197 publications

(132 citation statements)

References 16 publications

(12 reference statements)

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“…The mutant sh2-7527, kindly provided by the late Oliver Nelson (University of Wisconsin, Madison), was described previously (Giroux and Hannah, 1994). The wild-type Sh2 allele used in this study was isolated originally from McClintock's a1-m3 stock (Giroux et al, 1996).…”

Section: Plant Materialsmentioning

confidence: 99%

“…One group, represented by the classic maize transposable elements, have terminal inverted repeats, duplicate host sequences upon integration, and transpose via DNA (Engels, 1983;Fedoroff, 1989). These elements usually leave characteristic footprints after excision (Doring and Starlinger, 1986;Nevers et al, 1986;Jin and Bennetzen, 1989;Singer et al, 1993;Giroux et al, 1996;Kunze et al, 1997). The second group, the retroelements, move through an RNA copy, are related to retroviruses, and include longterminal repeat and non-long-terminal repeat retrotransposons (Wessler et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

“…This mutation, sh2-7527 , arose spontaneously in a conventional maize breeding program within the shrunken2 ( Sh2 ) gene of maize. The locus encodes the large subunit of ADP-Glc pyrophosphorylase, a key regulatory enzyme in the starch biosynthetic pathway (Giroux et al, 1996;Smidansky et al, 2002). Like Helitrons , this insertion is large, has no sequence or structural similarity to previously described cutand-paste or copy-and-paste transposable elements, lacks terminal repeats, did not duplicate host sequences upon insertion, was inserted within a host dinucleotide AT, is flanked by a TC 5 Ј terminus and a CTRR 3 Ј terminus, and contains two short palindromic sequences near the 3 Ј terminus that potentially could form a 20-bp hairpin.…”

Section: Introductionmentioning

confidence: 99%

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The Maize Genome Contains a Helitron Insertion

et al. 2003

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The maize mutation sh2-7527 was isolated in a conventional maize breeding program in the 1970s. Although the mutant contains foreign sequences within the gene, the mutation is not attributable to an interchromosomal exchange or to a chromosomal inversion. Hence, the mutation was caused by an insertion. Sequences at the two Sh2 borders have not been scrambled or mutated, suggesting that the insertion is not caused by a catastrophic reshuffling of the maize genome. The insertion is large, at least 12 kb, and is highly repetitive in maize. As judged by hybridization, sorghum contains only one or a few copies of the element, whereas no hybridization was seen to the Arabidopsis genome. The insertion acts from a distance to alter the splicing of the sh2 pre-mRNA. Three distinct intron-bearing maize genes were found in the insertion. Of most significance, the insertion bears striking similarity to the recently described DNA helicase-bearing transposable elements termed Helitrons . Like Helitrons , the inserted sequence of sh2-7527 is large, lacks terminal repeats, does not duplicate host sequences, and was inserted between a host dinucleotide AT. Like Helitrons , the maize element contains 5 TC and 3 CTRR termini as well as two short palindromic sequences near the 3 terminus that potentially can form a 20-bp hairpin. Although the maize element lacks sequence information for a DNA helicase, it does contain four exons with similarity to a plant DEAD box RNA helicase. A second Helitron insertion was found in the maize genomic database. These data strongly suggest an active Helitron in the present-day maize genome.

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Section: Plant Materialsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Maize Genome Contains a Helitron Insertion

et al. 2003

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“…It was shown previously that reduced AGPase sensitivity to Pi causes increased maize seed weight (Giroux et al, 1996). A site-specific, in vivo transposon mutagenesis system was employed to cause mutations within a region of the maize large subunit thought important in allosteric regulation.…”

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confidence: 99%

Characterization of an Autonomously Activated Plant ADP-Glucose Pyrophosphorylase

et al. 2008

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ADP-glucose pyrophosphorylase (AGPase) catalyzes the rate-limiting step in starch biosynthesis in plants and changes in its catalytic and/or allosteric properties can lead to increased starch production. Recently, a maize (Zea mays)/potato (Solanum tuberosum) small subunit mosaic, MP ], containing the first 198 amino acids of the small subunit of the maize endosperm enzyme and the last 277 amino acids from the potato tuber enzyme, was expressed with the maize endosperm large subunit and was reported to have favorable kinetic and allosteric properties. Here, we show that this mosaic, in the absence of activator, performs like a wild-type AGPase that is partially activated with 3-phosphoglyceric acid (3-PGA). In the presence of 3-PGA, enzyme properties of Mos(1-198)/SH2 are quite similar to those of the wild-type maize enzyme. In the absence of 3-PGA, however, the mosaic enzyme exhibits greater activity, higher affinity for the substrates, and partial inactivation by inorganic phosphate. The Mos(1-198)/SH2 enzyme is also more stable to heat inactivation. The different properties of this protein were mapped using various mosaics containing smaller portions of the potato small subunit. Enhanced heat stability of Mos(1-198) was shown to originate from five potato-derived amino acids between 322 and 377. These amino acids were shown previously to be important in small subunit/large subunit interactions. These five potato-derived amino acids plus other potato-derived amino acids distributed throughout the carboxyl-terminal portion of the protein are required for the enhanced catalytic and allosteric properties exhibited by Mos(1-198)/SH2.

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“…This reaction is an important regulatory step in the biosyntheses of glycogen and starch in bacteria and plants respectively. [1][2][3][4][5][6][7][8] The activities of bacterial and plant AGPases are allosterically regulated by sugar metabolites. Bacterial AGPases are activated by pyruvate (PYR), fructose 6-phosphate (F6P), and fructose 1,6-bisphosphate (F16BP), and are inhibited by AMP.…”

mentioning

confidence: 99%