A Stimulatory Action of Indole-3-Acetic Acid on the Uptake of Amino-Acids by Plant Cells

Nature ◽  
1956 ◽  
Vol 177 (4510) ◽  
pp. 658-659 ◽  
Author(s):  
LEONORA REINHOLD ◽  
R. G. POWELL
2016 ◽  
Vol 6 (1) ◽  
pp. 18
Author(s):  
Ragapadmi S Purnamaningsih

<p>Introduction of DefH9-iaaM and DefH9-RI-iaaM Gene<br />Into Tomato Genome Using Agrobacterium tumefaciens.<br />Ragapadmi Purnamaningsih. Plant genetic improvement<br />can be conducted through genetic engineering.<br />Parthenocarpic fruit production could increase fruit<br />production and its qulities. IAA genes were introduced into<br />three tomato cultivars Ratna, Opal and LV 6117 using two<br />constract genes DefH9-iaaM and DefH9-RI-iaaM. The iaaM<br />gene is able to increase auxin biosynthesis in transgenic<br />plant cells and organs because indol-eacetamide,<br />synthesized by the product of the iaaM gene, is converted<br />either chemically or enzimatically to indole-3-acetic acid<br />(IAA), while the promotor DefH9 enable IAA gene expressed<br />specifically in the ovules. The objectives of this experiment<br />was to identify gene introduction into plant genom of three<br />tomato cultivars. The factors tested were two constract of<br />IAA genes (DefH9-iaaM or DefH9-RI-iaaM), tomato cultivars<br />(Ratna, Opal, and LV 6117) and time of explant inoculation<br />(5, 15, 30 minute). The result showed that the best time<br />inoculation was 5 minute. Otherwise three tomato cultivars<br />response better to DefH9-RI-iaaM than DefH9-iaaM. The total<br />efficiency of regeneration and total efficiency of<br />transformation of both genes were 25.38% and 20.32%. PCR<br />analysis showed that 10 plant have positive PCR, were 1<br />plant carried (Opal) DefH9-iaaM gene and 9 plant (Ratna,<br />Opal, LV 6117) carried DefH9-RI-iaaM gene.</p>


1993 ◽  
Vol 20 (5) ◽  
pp. 527 ◽  
Author(s):  
HM Nonhebel ◽  
TP Cooney ◽  
R Simpson

The study of indole-3-acetic acid synthesis has undergone something of a revival recently in an attempt to understand the control of IAA levels. Results are, however, contradictory with three separate hypotheses emerging. Our own work supports older evidence for L-tryptophan as the IAA precursor and appears to simplify the metabolism of tryptophan to IAA. Work comparing incorporation of 2H from 2H2O into IAA, tryptophan, tryptamine and indole-3-pyruvate in tomato shoots showed that the indole-3-pyruvate became labelled at a rate compatible with it being the sole intermediate between tryptophan and indole-3-acetaldehyde. Results also showed that tryptamine was not involved in IAA synthesis although it was present. Indole-3-acetaldoxime was not detected in tomato shoots. An aromatic aminotransferase able to catalyse the synthesis of indole-3-pyruvate has been purified from mung beans. This enzyme was separated from aspartate aminotransferase and is fairly specific for aromatic L-amino acids. Other work, however, has implicated D-tryptophan as a more direct precursor than the L-enantiomer. A D-tryptophan aminotransferase has been isolated from dark grown pea seedlings. Finally, other recent work has indicated the existence of an alternative biosynthetic route to IAA which does not involve tryptophan. These results are reviewed in this paper and the apparent contradictions between them discussed.


1974 ◽  
Vol 31 (3) ◽  
pp. 357-365 ◽  
Author(s):  
S. Kristensen

1. Ruminal metabolism of labelled phenylacetic acid, 4-hydroxyphenylacetic acid, indole-3-acetic acid, glucose, shikimic acid, phenol, and serine was studied in vitro by short-term incubation with special reference to incorporation rates into aromatic amino acids.2. Earlier reports on reductive carboxylation of phenylacetic acid and indole-3-acetic acid in the rumen were confirmed and the formation of tyrosine from 4-hydroxyphenylacetic acid was demonstrated for the first time.3. The amount of phenylalanine synthesized from phenylacetic acid was estimated to be 2 mg/1 rumen contents per 24 h, whereas the amount synthesized from glucose might be eight times as great, depending on diet.4. Shikimic acid was a poor precursor of the aromatic amino acids, presumably owing to its slow entry into rumen bacteria.5. A slow conversion of phenol into tyrosine was observed.


2005 ◽  
Vol 17 (2) ◽  
pp. 616-627 ◽  
Author(s):  
Paul E. Staswick ◽  
Bogdan Serban ◽  
Martha Rowe ◽  
Iskender Tiryaki ◽  
Marién T. Maldonado ◽  
...  

Plants ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2034
Author(s):  
Hugo A. Méndez-Hernández ◽  
Ana O. Quintana-Escobar ◽  
Miguel A. Uc-Chuc ◽  
Víctor M. Loyola-Vargas

Auxin plays a central role in growth and plant development. To maintain auxin homeostasis, biological processes such as biosynthesis, transport, degradation, and reversible conjugation are essential. The Gretchen Hagen 3 (GH3) family genes codify for the enzymes that esterify indole-3-acetic acid (IAA) to various amino acids, which is a key process in the induction of somatic embryogenesis (SE). The GH3 family is one of the principal families of early response to auxin genes, exhibiting IAA-amido synthetase activity to maintain optimal levels of free auxin in the cell. In this study, we carried out a systematic identification of the GH3 gene family in the genome of Coffea canephora, determining a total of 18 CcGH3 genes. Analysis of the genetic structures and phylogenetic relationships of CcGH3 genes with GH3 genes from other plant species revealed that they could be clustered in two major categories with groups 1 and 2 of the GH3 family of Arabidopsis. We analyzed the transcriptome expression profiles of the 18 CcGH3 genes using RNA-Seq analysis-based data and qRT-PCR during the different points of somatic embryogenesis induction. Furthermore, the endogenous quantification of free and conjugated indole-3-acetic acid (IAA) suggests that the various members of the CcGH3 genes play a crucial role during the embryogenic process of C. canephora. Three-dimensional modeling of the selected CcGH3 proteins showed that they consist of two domains: an extensive N-terminal domain and a smaller C-terminal domain. All proteins analyzed in the present study shared a unique conserved structural topology. Additionally, we identified conserved regions that could function to bind nucleotides and specific amino acids for the conjugation of IAA during SE in C. canephora. These results provide a better understanding of the C. canephora GH3 gene family for further exploration and possible genetic manipulation.


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