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

Hesse, Thomas; Feldwisch, Joachim; Balshüsemann, Dirk; Bauw, Guy; Puype, Magda; Vandekerckhove, Joël; Löbler, Marian; Klämbt, Dieter; Schell, Jeff; Palme, Klaus

doi:10.1002/j.1460-2075.1989.tb08380.x

Cited by 209 publications

(46 citation statements)

References 52 publications

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“…The function of auxin-binding protein remains unknown, although it is widely assumed that the protein may be involved in signal transduction of plant hormone auxin. Auxinbinding protein is localized primarily in the ER as if it were a reticuloplasmin (64,65), although a small fraction of the auxinbinding protein is secreted to the cell surface (59,66,67) with its KDEL sequence intact (59). The binding of ligand, auxin, may alter the exposure of the KDEL sequence, and this could change the trafficking of the protein (68) so that its removal is not necessary to allow its exit from the ER.…”

Section: Discussionmentioning

confidence: 99%

Posttranslational Removal of the Carboxyl-terminal KDEL of the Cysteine Protease SH-EP Occurs Prior to Maturation of the Enzyme

Okomoto

Minamikawa

Edward

et al. 1999

Journal of Biological Chemistry

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SH-EP is a cysteine protease from germinating mung bean (Vigna mungo) that possesses a carboxyl-terminal endoplasmic reticulum (ER) retention sequence, KDEL. In order to examine the function of the ER retention sequence, we expressed a full-length cDNA of SH-EP and a minus-KDEL control in insect Sf-9 cells using the baculovirus system. Our observations on the synthesis, processing, and trafficking of SH-EP in Sf-9 cells suggest that the KDEL ER-retention sequence is posttranslationally removed either while the protein is still in the ER or immediately after its exit from the ER, resulting in the accumulation of proSH-EP minus its KDEL signal. It is this intermediate form that appears to progress through the endomembrane system and is subsequently processed to form mature active SH-EP. The removal of an ER retention may regulate protein delivery to a functional site and present an alternative role for ER retention sequences in addition to their well established role in maintaining the protein composition of the ER lumen.SH-EP is a thiol protease expressed in germinating mung bean (Vigna mungo) cotyledons (1-3) that is among a large number of similar cysteine proteases that are synthesized after germination in order to degrade seed storage proteins (2, 4 -10). All cysteine proteases are initially synthesized as larger precursor proteins with NH 2 -terminal prodomains of approximately 120 amino acids (11). The prodomain is an inhibitor of the protease (12) and is essential in the correct folding of the protein (13). Processing of the proenzyme occurs by self-catalysis (14) in post-Golgi compartments of the secretory system. With intracellular proteases, this processing occurs in the lytic compartment (lysosomes or vacuoles) (15); with extracellular proteases, the processing occurs during secretion (16). Targeting to the correct compartment for processing is mediated by a peptide (17) or phosphomannose (18) targeting signal on the NH 2 -terminal precursor domain that is recognized by a specific receptor that is presumed to be localized in the Golgi apparatus (19,20) to target the protein to the activating compartment.SH-EP is unusual because it and a few closely related thiol proteases (21-23) are the only cysteine proteases known to possess a carboxyl-terminal ER 1 retention sequence KDEL (24 -26). Although papain superfamily proteases are widely distributed among eukaryotes (27, 28), only these plant cysteine proteases have been identified as possessing a carboxylterminal ER retention sequence. Several other legume cysteine proteases have been cloned that do not possess a KDEL tail (28 -34), indicating that even among legumes and more broadly in plants these KDEL-proteases appear to constitute a special class. Plant cells utilize both HDEL and KDEL as ER retention sequences (35)(36)(37)(38). The presence of a carboxyl-terminal KDEL in SH-EP raises a question as to whether this sequence is functional in vivo. A papain superfamily cysteine protease would appear to be an unusual putative constituent of the ER lumen, ...

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Section: Discussionmentioning

confidence: 99%

Posttranslational Removal of the Carboxyl-terminal KDEL of the Cysteine Protease SH-EP Occurs Prior to Maturation of the Enzyme

Okomoto

Minamikawa

Edward

et al. 1999

Journal of Biological Chemistry

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“…This modification would result in a molecular mass of the unglycosylated ABP of -18.5 kd which is in accordance with the experimental data of Lobler et al (1987). It has to be mentioned that, up to now, all ABP preparations from corn coleoptiles did not contain a homogeneous protein except for the use of analytical methods (Hesse et al, 1989). Even affinity chromatography methods of purification with immobilized auxin analogs result in at least two protein species of slightly different sizes ( Figure 5; Shimomura et al, 1986).…”

Section: Resultsmentioning

confidence: 99%

“…This plasmid, pGem.ABP, allows synthesis of sense RNA with SP6 RNA polymerase. The transcription resulted in a single RNA species of -850 bases, which directed the synthesis of a 22 kd protein in a wheat germ translation system ( selected by oligonucleotides designed from the amino acid sequence of the purified main component of ABP (Hesse et al, 1989 Napier et al, 1988). This finding is consistent with previous results.…”

Section: Resultsmentioning

confidence: 99%

cDNA clones of the auxin-binding protein from corn coleoptiles (Zea mays L): isolation and characterization by immunological methods

Tillmann¹

1989

Trends in Genetics

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“…Quinclorac inhibited maize growth more strongly than IAA and NAA, yet [3H]NAA binding activity of control was 40-45 pmol/mg protein. The length of the control maize shoot was [13][14][15] cm.…”

Section: Resultsmentioning

confidence: 99%

Competition by Auxin-Type Herbicides for NAA Binding to Maize Auxin Binding Protein

Mito¹,

Sori²,

Miyakado³

et al. 1991

J. Pestic. Sci.

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Binding of auxin-type herbicides to maize membrane-bound auxin binding protein was compared with their physiological activities.There was a good correlation between the binding and the growth promoting activity of the herbicides, but the ethylene production or the inhibition of shoot growth did not completely correlate with the binding. Benazolin[4-chloro-2-oxobenzothiazolin-3-yl-acetic acid] did not bind to maize auxin binding protein, but it stimulated ethylene production.Quinclorac [3, 7-dichloro-8-quinolinecarboxylic acid] did not bind to maize auxin binding protein, but it strongly inhibited maize shoot growth. These results may suggest that the stimulation of ethylene production and the growth inhibition by auxin-type herbicides are not triggered by their binding to the putative maize membrane-bound auxin receptor.

show abstract

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

Cited by 209 publications

References 52 publications

Posttranslational Removal of the Carboxyl-terminal KDEL of the Cysteine Protease SH-EP Occurs Prior to Maturation of the Enzyme

Posttranslational Removal of the Carboxyl-terminal KDEL of the Cysteine Protease SH-EP Occurs Prior to Maturation of the Enzyme

cDNA clones of the auxin-binding protein from corn coleoptiles (Zea mays L): isolation and characterization by immunological methods

Competition by Auxin-Type Herbicides for NAA Binding to Maize Auxin Binding Protein

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