Molecular cloning and structural analysis of a gene from Zea mays (L) coding for a putative receptor for the plant hormone auxin

Hesse, Thomas

doi:10.1016/0168-9525(89)90163-7

Cited by 49 publications

(63 citation statements)

References 28 publications

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“…There are two known plant proteins with KDEL at their carboxyl termini. They are the auxin-binding protein from maize (Hesse et al, 1989;lnohara et al, 1989) and the sulphydryl-endopeptidase of Vigna mungo (Akasofu etal., 1989). The auxin-binding protein is known to be located in the ER and consistent with this, it contains a cluster of acidic residues in the terminal region.…”

Section: Discussionmentioning

confidence: 99%

Vicilin with carboxy‐terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants

et al. 1992

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SummaryGene constructs were designed to test the effect of the endoplasmic reticulum (El?)-targeting signal, KDEL, on the level of accumulation of a foreign protein in transgenic plants. The gene for the pea seed protein vicilin was modified by the addition of a sequence coding for this tetrapeptide at its carboxyl terminus. The altered gene was placed under the control of a CaMV 35s promoter and its expression in the leaves of both tobacco and lucerne (alfalfa) was compared with that of an equivalent vicilin construct lacking the KDELcoding sequence. The presence of the ER-targeting signal led to a greatly enhanced accumulation of the heterologous protein. In lucerne and tobacco leaves, the level of vicilin-KDEL protein was 20 and 100 times greater than that of the unmodified vicilin, respectively. These differences in expression level could not be explained by corresponding differences in the steadystate levels or the translatability of the mRNAs. However, when the stability of vicilin and vicilin-KDEL proteins was compared in their respective transgenic hosts, unmodified vicilin was found to be degraded with a half-life of 4.5 h while vicilin-KDEL was much more stable with a half-life of more than 48 h. lmmunogold labelling of leaf tissues from transgenic lucerne and tobacco showed the presence of vicilin associated with large aggregates within the ER lumen of vicilin-KDEL plants. No such aggregates were detected in transgenic plants expressing wild-type vicilin.It is concluded that the carboxy-terminal KDEL caused the retention of the modified vicilin in the ER, and that this retention led to the increased stability and higher level of accumulation of vicilin-KDEL in leaves of transgenic plants.

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Section: Discussionmentioning

confidence: 99%

Vicilin with carboxy‐terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants

et al. 1992

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“…More progress has been made in understanding the molecular basis for the action of auxin than cytokinin because auxin stimulates rapid and easily measured physiological events. Auxin responses are thought to involve receptors that may be represented by auxin binding proteins such as ABPl (Hesse et al, 1989;lnohara et al, 1989). Antibodies specific to ABPl reduce auxin-induced membrane hyperpolarization, and addition of ABPl to tobacco protoplasts further sensitizes the membrane response (Barbier-Brygoo et al, 1989, 1991.…”

Section: Introductionmentioning

confidence: 99%

Cytokinins and auxins control the expression of a gene in Nicotiana plumbaginifolia cells by feedback regulation.

et al. 1992

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Both cytokinin (N6-benzyladenine [BA]) and auxin (2,4-dichlorophenoxyacetic acid [2,4-D]) stimulate the accumulation of an mRNA, represented by the cDNA pLS216, in Nicotiana plumbaginifolia suspension culture cells. The kinetics of RNA accumulation were different for the two hormones; however, the response to both was transient, and the magnitude of the response was dose dependent. Runoff transcription experiments demonstrated that the transient appearance of the RNA could be accounted for by feedback regulation of transcription and not by the induction of an RNA degradation system. The feedback mechanism appeared to desensitize the cells to further exposure of the hormone. In particular, cells became refractory to the subsequent addition of 2,4-D after the initial RNA accumulation response subsided. A very different response was observed when the second hormone was added to cells that had been desensitized to the first hormone. Under such conditions, BA produced a heightened response in cells desensitized to 2,4-D and vice versa. These findings support a model in which cytokinin further enhances the auxin response or prevents its feedback inhibition. The hormone-induced RNA accumulation was blocked by the protein kinase inhibitor staurosporin. On the other hand, the protein phosphatase inhibitor okadaic acid stimulated expression, and, in particular, okadaic acid was able to stimulate RNA accumulation in cells desensitized to auxin. This suggests that hormone activation involves phosphorylation of critical proteins on the hormone signaling pathway, whereas feedback inhibition may involve dephosphorylation of these proteins. The sequence of pLS216 is similar to genes in other plants that are stimulated by multiple agonists such as auxins, elicitors, and heavy metals, and to the gene encoding the stringent starvation protein in Escherichia coli. It is proposed that this gene family in various plants be called multiple stimulus response (msr) genes.

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“…The bestcharacterized of these auxin binding proteins is ABP1, which was discovered almost 40 years ago (Hertel et al, 1972). ABP1 was purified as a soluble protein from a maize coleoptile membrane fraction and consisted of 201 amino acid residues, including an N-terminal hydrophobic signal sequence for translocation to the endoplasmic reticulum and a C-terminal KDEL amino acid sequence − 48 − for endoplasmic reticulum retention (Hesse et al, 1989;Tillmann et al, 1989). A binding assay using radiolabeled auxin suggested that ABP1 effectively binds to 1-NAA rather than IAA and shows low affinity to 2,4-D (Löbler & Klämbt, 1985).…”

Section: Auxin Binding Protein 1 (Abp1)mentioning

confidence: 99%

New Insights to Auxin Signaling through The Use of Small Molecules

Biswas

Oono

2011

Biol. Sci. Space

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Elucidating the perception mechanism of auxin has been a long-standing goal in plant biology. To und e rst and the m e chanism , studies on the chemical structure and activity relationships of auxin-related small molecules have been done for more than half a century. Today, aided mainly by Arabidopsis genetics, researchers have identified the core complexes for auxin perception, including the auxin receptors TIR1/AFBs, SKP2 and ABP1. Forward chemical screening using auxin response markers has also played an important role in identifying small molecules affecting the auxinsignaling pathways and led to the screening of additional auxin related mutants. This approach has helped in identifying several unique molecular components of the auxinsignaling pathways, and discovering that would have been impossible using traditional screening of mutants against auxin. This review is focused on recently acquired knowledge of multiple auxin signaling pathways and related small compounds that can be used to dissect auxin signal transduction pathways. In addition, the involvement of distinct auxinsignaling machineries during gravity response is discussed.

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Molecular cloning and structural analysis of a gene from Zea mays (L) coding for a putative receptor for the plant hormone auxin

Cited by 49 publications

References 28 publications

Vicilin with carboxy‐terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants

Vicilin with carboxy‐terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants

Cytokinins and auxins control the expression of a gene in Nicotiana plumbaginifolia cells by feedback regulation.

New Insights to Auxin Signaling through The Use of Small Molecules

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