Biosynthesis, conjugation, catabolism and homeostasis of indole-3-acetic acid in Arabidopsis thaliana

Ljung, Karin; Hull, Anna K.; Kowalczyk, Mariusz; Marchant, Alan; Celenza, John L.; Cohen, Jerry D.; Sandberg, Göran

doi:10.1007/978-94-010-0377-3_1

Cited by 144 publications

(218 citation statements)

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“…Here, using a combination of liquid chromatography, gas chromatography, and mass spectrometry on axenic cultures, we showed that IAA was present in low, but significant, amounts in E. siliculosus sporophytes. IPA and ICA, likely to be decarboxylated degradation products of IAA (Ljung et al, 2002), were also detected. The levels of IAA quantified in E. siliculosus were similar to those found in the brown alga F. vesiculosus (Basu et al, 2002).…”

Section: Synthesis and Transport Of Auxin In E Siliculosusmentioning

confidence: 99%

Auxin Metabolism and Function in the Multicellular Brown AlgaEctocarpus siliculosus

et al. 2010

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Ectocarpus siliculosus is a small brown alga that has recently been developed as a genetic model. Its thallus is filamentous, initially organized as a main primary filament composed of elongated cells and round cells, from which branches differentiate. Modeling of its early development suggests the involvement of very local positional information mediated by cell-cell recognition. However, this model also indicates that an additional mechanism is required to ensure proper organization of the branching pattern. In this paper, we show that auxin indole-3-acetic acid (IAA) is detectable in mature E. siliculosus organisms and that it is present mainly at the apices of the filaments in the early stages of development. An in silico survey of auxin biosynthesis, conjugation, response, and transport genes showed that mainly IAA biosynthesis genes from land plants have homologs in the E. siliculosus genome. In addition, application of exogenous auxins and 2,3,5-triiodobenzoic acid had different effects depending on the developmental stage of the organism, and we propose a model in which auxin is involved in the negative control of progression in the developmental program. Furthermore, we identified an auxin-inducible gene called EsGRP1 from a small-scale microarray experiment and showed that its expression in a series of morphogenetic mutants was positively correlated with both their elongated-to-round cell ratio and their progression in the developmental program. Altogether, these data suggest that IAA is used by the brown alga Ectocarpus to relay cell-cell positional information and induces a signaling pathway different from that known in land plants.

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Section: Synthesis and Transport Of Auxin In E Siliculosusmentioning

confidence: 99%

Auxin Metabolism and Function in the Multicellular Brown AlgaEctocarpus siliculosus

et al. 2010

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“…For example, in Arabidopsis thaliana, less than 5% of auxins are found in the active free form with the remaining 95% primarily conjugated to either amino acids or peptides. 13 Enzymatic conversion of unconjugated JA and IAA into the corresponding amino acid conjugates drastically alters hormone action (Fig. 1).…”

Section: Modulating Plant Hormones By Enzyme Actionmentioning

confidence: 99%

Modulating plant hormones by enzyme action

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Chen

et al. 2010

Plant Signaling & Behavior

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“…Similarly, indole-3-acetic acid (IAA)-Glc synthesized by indole-3-acetic acid glucosyltransferase serves as an activated form of IAA, which is used in a transesterification reaction to form IAA-inositol (Michalczuk and Bandurski, 1982;Jackson et al, 2001Jackson et al, , 2002Ljung et al, 2002). This latter reaction is analogous to sinapoylmalate biosynthesis and preliminary indications suggest that it may be catalyzed by an SCPL enzyme (Kowalczyk et al, 2003).…”

Section: Candidate Reactions For Scpl Acyltransferases Can Be Found Tmentioning

confidence: 99%

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

2005

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The Arabidopsis (Arabidopsis thaliana) genome encodes a family of 51 proteins that are homologous to known serine carboxypeptidases. Based on their sequences, these serine carboxypeptidase-like (SCPL) proteins can be divided into several major clades. The first group consists of 21 proteins which, despite the function implied by their annotation, includes two that have been shown to function as acyltransferases in plant secondary metabolism: sinapoylglucose:malate sinapoyltransferase and sinapoylglucose:choline sinapoyltransferase. A second group comprises 25 SCPL proteins whose biochemical functions have not been clearly defined. Genes encoding representatives from both of these clades can be found in many plants, but have not yet been identified in other phyla. In contrast, the remaining SCPL proteins include five members that are similar to serine carboxypeptidases from a variety of organisms, including fungi and animals. Reverse transcription PCR results suggest that some SCPL genes are expressed in a highly tissue-specific fashion, whereas others are transcribed in a wide range of tissue types. Taken together, these data suggest that the Arabidopsis SCPL gene family encodes a diverse group of enzymes whose functions are likely to extend beyond protein degradation and processing to include activities such as the production of secondary metabolites.Serine carboxypeptidases (SCPs) are members of the a/b hydrolase family of proteins, which make use of a Ser-Asp-His catalytic triad to cleave the carboxyterminal peptide bonds of their protein or peptide substrates (Hayashi et al., 1973(Hayashi et al., , 1975Bech and Breddam, 1989;Liao and Remington, 1990;Liao et al., 1992;Ollis et al., 1992). Proteins that contain this catalytic triad and are otherwise homologous to SCPs have been found in a variety of organisms (Doi et al., 1980;Kim and Hayashi, 1983;Breddam, 1986;Baulcombe et al., 1987;Galjart et al., 1988;Bradley, 1992;Degan et al., 1994;Endrizzi et al., 1994;Wajant et al., 1994;Jones et al., 1996;Li and Steffens, 2000). Many of these serine carboxypeptidase-like (SCPL) proteins have been annotated as peptidases based only on this shared sequence similarity; however, studies have shown that some of them function not as peptidases, but as acyltransferases and lyases (Wajant et al., 1994;Lehfeldt et al., 2000;Li and Steffens, 2000;Shirley et al., 2001). For example, several SCPL proteins have been shown to catalyze the production of plant secondary metabolites involved in herbivory defense and UV protection (Wajant et al., 1994;Lehfeldt et al., 2000;Li and Steffens, 2000), including the hydroxynitrile lyase from Sorghum bicolor (SbHNL) necessary for cyanogenesis, and the acyltransferases in wild tomato (Lycopersicon pennellii) that catalyze the formation 2,3,4-isobutyryl-Glc (Wajant et al., 1994;Lehfeldt et al., 2000). Two enzymes in Arabidopsis (Arabidopsis thaliana) responsible for sinapate ester biosynthesis are also SCPL proteins. Sinapoylglucose:malate sinapoyltransferase (SMT) catalyzes the formation of s...

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Biosynthesis, conjugation, catabolism and homeostasis of indole-3-acetic acid in Arabidopsis thaliana

Cited by 144 publications

References 134 publications

Auxin Metabolism and Function in the Multicellular Brown AlgaEctocarpus siliculosus

Auxin Metabolism and Function in the Multicellular Brown AlgaEctocarpus siliculosus

Modulating plant hormones by enzyme action

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family

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