Category:Team McClintock

Figures 1A and D show that quantitatively (by total leaves) and through photo comparison that hos1 mutants exhibit early flowering phenotype at both 23 and 16°C under LD conditions when compared to the C24 ecotype background. These mutants display an ambient temperature-insensitive phenotype.

Figure 5B demonstrates in vitro ZmSNAC1 phosphorylation by ZmOST1. Figure 5C illustrates that kinase activity is lost in extracts from the ost1-2allele and recovered in extracts of the ZmOST1/ost1-2 complemented line (Arabidopsis).

Figure 3D illustrates that three transgenic Arabidopsis lines with overexpression of GsWRKY20 were able to germinate much faster than wild type when exposed to 0.8 μM ABA. Figure 3F shows that overexpressing GsWRKY20 Arabidopsis lines had significantly higher percentages of leaf opening and greening at different ABA concentrations than wild type. Fig 8

Figure 5B shows that overexpression of DgBRC1 in brc1-1 Arabidopsis mutant lines was indistinguishable from the wild type lateral branching. Table S2 shows that the number of rosette branches was reduced in DgBRC1 overexpressing wild type plants.

Figure 4E shows that three GPX3 post-transcriptional knockdown transgenic lines exhibit shorter root lengths when compared to control plants normalized for GPX3 expression.

Figure 4D shows that three GPX3 post-transcriptional knockdown transgenic lines exhibit shorter shoot lengths when compared to control plants normalized for GPX3 expression.

Figure 3A shows that atairp3/log2-2 knockout and 35S:AtAIRP3-RNAi knockdown mutants exhibit reduced ABA-mediated inhibition of germination. Figure 3B shows that atairp3/log2-2 mutants have a higher radical emergence percentage than wild type at different concentrations of abscisic acid, as well as substantially higher percentages of cotyledon greening.

Figure 3C shows that atairp3/log2-2 knockout and 35S:AtAIRP3-RNAi knockdown mutants exhibit impaired stomatal closure response to different concentrations of abscisic acid when compared to wild type. Figure 3D graphically quantifies this impaired response.

Figure 1C shows partial phenotypic ost1-2 complementation by ZmOST1 in drought signaling through comparing temperature of detached leaves by infrared thermography.

Figure 3D shows that under blue light, the cych;1 RNAi mutants had a much smaller stomatal aperature width than wild type, similar to cry1 and cry2 mutant controls.

Figure 2A shows the drought response of soil-grown cych;1 RNAi mutants plants compared to wt: mutant plants exhibit less wilting. Figure 2B shows that after re-watering, 3% of wt plants survived compared to 70% of mutants. Figure 2C shows that detached leaves of mutants lose water more slowly compared to wt.

Figure 4C and table II show that during reproductive growth, mos1 inflorescence produced approximately twice the number of lateral spikelets compared to wild type.

Figure 5C shows that in mos1 the branch axillary meristems formed lateral spikelets as the branches transitioned to the awn initiation stage.

Figures 1a-c demonstrate delayed silique senescence in atnap knockout plants when compared to age-matched wildtype.

Figure 2

Figure 5A shows a Western blot analysis in amiRNA-HAM1 (HAM1 knockdown) lines compared to wildtype that demonstrates a significant decrease in global H4K5 acetylation. In contrast, H4K5 acetylation was significantly increased in HAM1-OE (over-expressed) lines.

Figure 1C shows that amiRNA-HAM1 (HAM1 knockdown) lines grew normally as the wild-type Col in the vegetative stage, but flowered earlier than Col under both LD and SD conditions.

Figure 3B demonstrates that HAM1-overexpressing transgenic plants (HAM1-OE) displayed a delayed flowering time phenotype compared to wild type, suggesting that HAM1 is a negative regulator of flowering.

Figure 6 shows radiolabeled Maize PyrR plastid localization.

Figure 3B shows that ZmPyrR complements reductase but not deaminase function of E. coli RibD.

Figure 4A shows the disappearance of 5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5’-P and Figure 4B shows the appearance of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5’-P in recombinant maize PyR. E. coli RibA, demonstrating pyrimidine reductase activity in vitro.