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Plant Physiol. (1998) 116: 1083-1089
Herbicide Safener-Binding Protein of Maize1
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ABSTRACT |
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Top
Abstract
Introduction
Methods
Results
Discussion
References
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Dichloroacetamide safeners protect maize (Zea mays L.) against injury from chloroacetanilide and thiocarbamate herbicides. Etiolated maize seedlings have a high-affinity cytosolic-binding site for the safener [3H](R,S)-3-dichloroacetyl-2,2,5-trimethyl-1,3-oxazol-idine ([3H]Saf), and this safener-binding activity (SafBA) is competitively inhibited by the herbicides. The safener-binding protein (SafBP), purified to homogeneity, has a relative molecular weight of 39,000, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and an isoelectric point of 5.5. Antiserum raised against purified SafBP specifically recognizes a 39-kD protein in etiolated maize and sorghum (Sorghum bicolor L.), which have SafBA, but not in etiolated wheat (Triticum aestivum L.), oat (Avena sativa L.), barley (Hordeum vulgare L.), tobacco (Nicotiana tabacum L.), or Arabidopsis, which lack SafBA. SafBP is most abundant in the coleoptile and scarcest in the leaves, consistent with the distribution of SafBA. SBP1, a cDNA encoding SafBP, was cloned using polymerase chain reaction primers based on purified proteolytic peptides. Extracts of Escherichia coli cells expressing SBP1 have strong [3H]Saf binding, which, like binding to the native maize protein, is competitively inhibited by the safener dichlormid and the herbicides S-ethyl dipropylthiocarbamate, alachlor, and metolachlor. SBP1 is predicted to encode a phenolic O-methyltransferase, but SafBP does not O-methylate catechol or caffeic acid. The acquisition of its encoding gene opens experimental approaches for the evaluation of the role of SafBP in response to the relevant safeners and herbicides.
Herbicide safeners, also known as antidotes, are used to protect
crops from herbicide injury (Hatzios, 1983
Etiolated maize seedlings contain a soluble, high-affinity-binding
activity (Kd, 0.12 µm) for a
tritiated form of the dichloroacetamide safener Saf (Fig. 1) (Walton
and Casida, 1995 To begin to address the question of the role of SafBA in the response
of maize seedlings to dichloroacetamide safeners and, possibly, to the
two classes of herbicides, we have further characterized SafBA. Here we
report the purification of SafBP, immunological studies of its tissue
and species distribution, and the cloning, sequencing, and expression
in Escherichia coli of a cDNA encoding SafBP.
Genotypes and sources of plant materials are as described by
Walton and Casida (1995) Binding Assay
INTRODUCTION
Top
Abstract
Introduction
Methods
Results
Discussion
References
, 1989; Fuerst, 1987). One
important class of safeners is the dichloroacetamides, such as
dichlormid, which are used in combination with thiocarbamate and
chloroacetanilide herbicides on maize (Zea mays L.) and
sorghum. Examples of these classes of compound are shown in Figure
1. Although it is well established that
in maize dichloroacetamide safeners elevate GSH levels and induce novel
GSH S-transferases, the mechanism by which they do so
is not known (Lay et al., 1975; Fuerst et al., 1993).
View larger version (8K):
[in a new window]
Figure 1.
Structures of compounds discussed in the text:
Saf, a dichloroacetamide herbicide safener; metolachlor, a
chloroacetanilide herbicide; and EPTC, a thiocarbamate herbicide.
). Although present in all tissues, SafBA is highest in
the coleoptile. There is a good correlation between inhibition of Saf
binding in vitro and safener action in vivo among a series of Saf
analogs, with dichlormid, a widely used dichloroacetamide safener,
being the strongest binding antagonist of any compound tested
(IC50, 10 nm). Chloroacetanilide and
thiocarbamate herbicides, which dichloroacetamide safeners protect
against, are also strong competitive inhibitors of Saf binding;
metolachlor and EPTC (Fig. 1) have IC50 values of
110 and 40 nm, respectively (Walton and Casida, 1995).
Despite their intensive use in agriculture for more than 30 years, the
mode of action of these herbicides is currently unknown.
MATERIALS AND METHODS
Top
Abstract
Introduction
Methods
Results
Discussion
References
. The Arabidopsis thaliana ecotype
was Columbia and the tobacco (Nicotiana tabacum) cultivar
was SR-1. Plants were grown in the dark on wet paper towels for 4 to
7 d.
. The sources of other chemicals are given by Walton
and Casida (1995). [3H]Saf binding was measured
by incubating extracts with approximately 400,000 cpm of
[3H]Saf in 50 mm Tris-HCl, pH 8.0, in a total volume of 1 mL for 60 min at 22°C. The extracts were then
filtered through glass-fiber filters (GF/A, Whatman) that had been
soaked in 0.3% (v/v) polyethylenimine and rinsed with water. The
radioactivity retained on the filters was measured by scintillation
counting (Walton and Casida, 1995).
Purification of SafBP
Coleoptiles of 4-d-old maize (Zea mays L.) seedlings grown in partial darkness on wet paper towels at 23°C (typically 5-10 g fresh weight) were ground in 50 mm Tris-HCl, pH 8.0, plus 0.4 m Suc (Walton and Casida, 1995). After being
filtered through cheesecloth, the extracts were treated by adding
(NH4)2SO4
to 50% saturation (0.295 g/mL), stirring for 30 min at 4°C, and
centrifuging for 15 min at 10,000g.
(NH4)2SO4
was again added to the supernatant to a final concentration of 70%
saturation (an additional 0.127 g/mL) and after stirring and
centrifugation the pellet was redissolved in chromatofocusing start
buffer (25 mm piperazine-HCl, pH 6.3) and desalted on a
gel-filtration column (PD-10, Pharmacia).
). Gels were stained with
Coomassie blue R-250. The Mr of the
proteins was estimated using prestained standards from GIBCO-BRL.
Gel-filtration chromatography was on a Superdex 200H 10/30 column
(Pharmacia) eluted with 0.1 m
KH2PO4, pH 7.0. The column
was equilibrated with gel-filtration standards from Bio-Rad.
Antibody Preparation and Immunoblotting
Purified SafBP (50 µg) was homogenized in Titermax adjuvant (CytRx, Norcross, GA) and injected subcutaneously into New Zealand White rabbits. Rabbits were bled after 42 and 56 d without any boost. The crude antiserum could be used to detect SafBP on immunoblots at a 1:16,000 dilution and was routinely used at a 1:5,000 dilution. SDS-PAGE gels were blotted onto 0.2-µm-pore nitrocellulose (Schleicher & Schuell) using a semidry Multiphor II apparatus according to the manufacturer's instructions (LKB, Pharmacia). Bound anti-SafBP antibody was detected using goat anti-rabbit IgG conjugated to alkaline phosphatase (Kirkegaard and Perry Laboratories, Gaithersburg, MD) (Scott-Craig et al., 1992).
Cloning of SBP1 cDNA by PCR
Routine nucleic acid manipulations were carried out as described by Sambrook et al. (1989) unless otherwise specified. The cDNA library,
made from poly(A+) RNA extracted from 12-d-old
etiolated maize seedlings of inbred B73 in vector 
ZipLox
(GIBCO-BRL), was obtained from Dr. Tim Helentjaris (Pioneer Hi-Bred
International, Johnston, IA).
RNA Analysis
View this table:
Table I.
Peptides obtained from SafBP
Peptides nos. 1 and 7 were obtained with trypsin and the others with
endoproteinase Asp-N. Parentheses indicate uncertain identification and
X indicates unknown. Amino acids in lowercase indicate differences
between the peptides and the deduced amino acid sequence of
SBP1. Peptide no. 5 was obtained twice from two digestions.
-GAYAAYTTYGGNATHGA, based on the amino acid
sequence DNFGIE in peptide no. 5 in Table
I) and primer 240 (5-GCNCCRAAYTCYTTNA,
based on the amino acid sequence LKEFGA in peptide no. 8 in Table I). Y
is C or T, N is any nucleotide, R is A or G, and H is A, T, or C. The
PCR products were separated by gel electrophoresis (0.7% agarose) and
blotted onto Nytran membranes (Schleicher & Schuell), and amplification
of the correct DNA sequence was tested by hybridization at 46°C with
radiolabeled primer 237 (5-GARTAYAARATHCTNAA, based on the amino acid
sequence EYKILK in peptide no. 8 in Table I).
-32P]ATP (DuPont), 10 units of T4
polynucleotide kinase (New England Biolabs), and buffer supplied by the
manufacturer. Hybridization was at 46°C. The approximately 500-bp PCR
product was cloned into the EcoRV site of pBluescript
(Stratagene), and was again confirmed by hybridization with probe 237 and by sequencing. The PCR product was used as a probe to isolate cDNAs
from the cDNA library and the entire sequence of both strands of one
was determined by automated fluorescence sequencing at the Michigan
State University Plant Research Laboratory Biochemistry Facility.
Sequences were analyzed by the BLAST (Altschul et al., 1990), DNASIS
(Hitachi, San Bruno, CA), and PILEUP programs (Genetics Computer Group,
1994).
. Total RNA (30 µg per lane) was fractionated by agarose
gel electrophoresis with formaldehyde and blotted onto Nytran membranes
(Schleicher & Schuell) (Sambrook et al., 1989). Hybridization was
carried out using the method of Singh and Jones (1984) at 65°C, and
filters were washed twice for 10 and 60 min at 65°C in 0.2× SSPE
(1× SSPE is 150 mm NaCl, 10 mm
NaH2PO4, and 1 mm EDTA, adjusted to pH 7.4 with NaOH) plus 0.2% SDS
before autoradiography. The size of the SBP1 mRNA was
estimated using a 0.24- to 9.5-kb RNA ladder (GIBCO-BRL). Equal loading
of lanes was confirmed by staining of the rRNA bands with ethidium
bromide.
Mapping
SBP1 was mapped using a set of recombinant inbred lines (Burr et al., 1994) provided by Dr. Benjamin Burr (Brookhaven National Laboratory, Upton, NY). Genomic DNA was extracted from 14-d-old plants
of the parental maize lines CM37 and T232 and the 50 recombinant lines
by the method of Hulbert and Bennetzen (1991). Eight micrograms of each
DNA sample was digested with EcoRI, separated on a 0.7% agarose gel, and blotted onto Nytran membranes. Hybridization and
washing were carried out as described above. The filters were then
stripped of probe and rehybridized with control probe BNL17.18 to
ensure that all samples were correctly labeled. The mapping data were
analyzed using INBRED software (Burr et al., 1994).
Expression of SafBP in Escherichia coli
Vector pZL1 (GIBCO-BRL), containing the SafBP cDNA clone, was digested with EcoRI and NotI, the 1.5-kb insert was cloned into the corresponding sites in the E. coli expression vector pET21c (Novagen, Madison, WI), and the construct was transformed into E. coli strain BL21(DE3) (Novagen). A 50-mL culture of this strain was grown at 37°C to an A600 of 0.5, at which point expression of the cDNA was induced with 1 mm IPTG. As a control, E. coli BL21(DE3) transformed with pET21c with no insert was grown in parallel. Samples (12.5 mL) were removed 0, 1, 2, and 3 h after induction, centrifuged, extracted by the freeze-thaw method according to Novagen, and centrifuged again to remove cell debris. SafBA was in the supernatant and was not further purified. Each sample was in a final volume of 5 mL of 50 mm Tris-HCl, pH 8.0, and 150 µL of this was used in the [3H]Saf-binding assay according to the method of Walton and Casida (1995).
OMT Assays
OMT assays were done using substrates from Sigma in a total volume of 500 µL containing 50 mm Tris-HCl, pH 8.0, 5 mm MgCl2, and 0.5 µCi S-[methyl-3H]-S-adenosyl Met (New England Nuclear; specific activity, 14.4 Ci/mmol). The addition of 2 mm DTT did not influence the activity. Reactions were incubated for 30 min at 21°C and stopped by the addition of 50 µL of 2 m HCl. Organic scintillation cocktail (5 mL) was then added and nonpolar radioactivity was determined directly (Preisig et al., 1989).
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RESULTS |
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Top
Abstract
Introduction
Methods
Results
Discussion
References
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Purification of SafBP
SafBA was purified by (NH4)2SO4 precipitation and three chromatographic steps to homogeneity, as judged by the presence of a single band on a one-dimensional SDS-polyacrylamide gel. SafBA is apparently the result of a protein (SafBP) with a molecular mass of 39 kD (Fig. 2). At no step in the purification was there any evidence of additional SafBPs. SafBP was shown by gel filtration to have a mass of 45 kD, and is therefore probably a monomer in its native state (data not shown). Based on Scatchard analysis showing that coleoptiles contain 55 pmol SafBA mg
1 protein (Walton and Casida, 1995), and
assuming that the binding stoichiometry is 1, it is estimated that
SafBP constitutes 0.2% of the total protein in the coleoptile.
[3H]Saf binding to purified SafBP was
competitively inhibited by thiocarbamate and chloroacetanilide
herbicides (data not shown), consistent with our earlier results with
SafBA in crude extracts (Walton and Casida, 1995).
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Immunological Analysis of SafBP
SafBP is present in the coleoptile, mesocotyl, and root, and to a lesser extent in the node and leaf (Fig. 3), consistent with earlier results showing that SafBA is most abundant in the coleoptile, present in the node, mesocotyl, and roots, and scarcest in the leaf (Walton and Casida, 1995). Antiserum raised against purified SafBP recognizes a
major 39-kD protein in maize and sorghum (Sorghum bicolor
L.), both of which contain SafBA, but not in wheat (Triticum
aestivum L.), oats (Avena sativa L.), or barley (Hordeum vulgare L.), which do not contain SafBA (Fig.
4; Walton and Casida, 1995). Arabidopsis
and tobacco, which also lack SafBP (J.D. Walton, unpublished results),
also lack a protein recognized by anti-SafBP antiserum (Fig. 4). The
nature of the cross-reacting protein(s) of approximately 30 kD is not
known (Fig. 4).
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Cloning of a cDNA Encoding SafBP
Based on the peptides obtained from proteolytic digests of SafBP shown in Table I, PCR was used to isolate three independent cDNAs encoding SafBP. All three cDNAs are approximately the same length and have the identical nucleotide sequences for at least 200 bp from either end in the regions where they overlap. The sequence of the longest cDNA, designated SBP1, has a single reading frame encoding a protein of 363 amino acids from the first in-frame Met to the first stop codon (Fig. 5). The predicted product is hydrophilic and has a Mr of 40,252 and a pI of 5.93, consistent with the measured biochemical properties of SafBP. All further experiments were done with SBP1.
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Expression of SafBP in E. coli
Analysis of the Sequence of SafBP
) and SafBP (Fig. 3) in this tissue.
View larger version (50K):
[in a new window]
Figure 6.
RNA blot of etiolated maize tissues. Lane 1, Coleoptile; lane 2, leaf; lane 3, node; lane 4, mesocotyl; and lane 5, root. The node included about 0.5 mm of tissue on either side. Equal loading (30 µg of total RNA) in each lane was confirmed by staining of the rRNA bands with ethidium bromide. The SBP1 mRNA
is approximately 1.5 kb.
to a location near the centromere of chromosome 2, between markers npi242C and rbcS2. SBP1 has
been entered on the maize map as marker msu1.
View this table:
Table II.
[3H]Saf binding in 50-µL extracts
of E. coli expressing SBP1
After growing to an A600 of 0.5, cells were
induced with IPTG and aliquots were harvested at the indicated times,
lysed, and centrifuged to remove cell debris. The final volume of each
extract was 5 mL. Control cells were transformed with the vector
without insert. Values are the average of duplicates.
View this table:
Table III.
Inhibition of [3H]Saf binding by
safeners and herbicides in extracts of E. coli expressing SBP1
The E. coli/SBP1 2-h time-point preparation from Table I was
used; protein content per sample was 20.9 µg. Values are the average
of duplicates.
) and TFASTA (Genetics Computer
Group, 1994) programs showed that SafBP is related to a number of known
or putative OMTs that methylate phenolic compounds such as catechol,
lignin precursors, and flavonoids. Significant BLAST scores were also
obtained against OMTs involved in methylation of inositol,
acetylserotonin, and hydroxyindole. Like SafBP, most of the similar
plant OMTs are soluble proteins of approximately 40 kD. The amino acid
sequence of SafBP is most closely related to that of a putative OMT in
barley that is induced by pathogens and UV light, with an overall amino
acid identity and similarity of 38 and 63%, respectively (Gregersen et
al., 1994; GenBank accession no. X77467). In contrast to the barley
OMT, however, SafBP is constitutively expressed and is not induced
further by safener or herbicide treatment (Walton and Casida, 1995;
Fig. 6) or by infection with a fungal pathogen (data not shown). The
sequence of SafBP is also related to that of a putative OMT, the mRNA
of which, ZRP4, is abundantly expressed in maize roots (34%
amino acid identity, 60% similarity; Held et al., 1993; GenBank
accession no. L14063) and might be involved in the biosynthesis of
suberin phenolics of the Casparian strip. Like SBP1,
ZRP4 is poorly expressed in leaves (Held et al., 1993).
; GenBank accession no.
U69554). SafBP is also related to a maize caffeic acid OMT (the product
of the bm3 gene), with 30% amino acid identity and 54%
similarity (Collazo et al., 1992; Vignols et al., 1995; GenBank
accession no. M73235), and to caffeic acid OMTs from alfalfa and
Monterey pine (Gowri et al., 1991; GenBank accession nos. M63853,
U39301, and U70873). The sequence of SafBP shows no significant
similarity to other classes of methyl transferases, including those
that use CoA derivatives as substrates (e.g. Pakusch and Matern, 1991), protein methylases, and DNA methylases.
). SafBP has a reasonable match to consensus motif II in the
correct position (consensus: [G/P]-
[T/Q][A/Y/F]DA[Y/V/I][I/F][L/V/C]; SafBP: PpAqtVvL,
starting at amino acid 258; matches are shown in uppercase), but
does not have the highly conserved central Asp residue. SafBP does not
have a good consensus motif III in the proper position relative to
motif II, but this motif is also not well conserved among known plant
phenolic OMTs. In this region, the plant OMTs and SafBP share the
sequence GKVI (starting at amino acid 295). However, SafBP lacks motif
I, which is not only the most highly conserved of the motifs among all
OMTs but is found in all of the plant phenolic OMTs.
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DISCUSSION |
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Top
Abstract
Introduction
Methods
Results
Discussion
References
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Based on its binding properties, SafBP is a good candidate for the
initial site of action of Saf and perhaps other dichloroacetamide safeners. It binds active compounds with high affinity and is abundant
in the coleoptile, an important tissue for the action of safeners and
herbicides (Hickey and Krueger, 1974). SafBP is present in maize and
sorghum, which respond to Saf, and absent in wheat, oat, and barley,
which do not respond. SafBP also strongly binds chloroacetanilide and
thiocarbamate herbicides in a competitive manner, suggesting that SafBP
might also be involved in the response to the herbicides against which
dichloroacetamide safeners protect.
).
).
reported that metolachlor-treated sorghum seedlings had
reduced lignification, consistent with the hypothesis that SafBP is
involved in the production of lignin precursors such as caffeic acid
and is the site of action of this herbicide, which binds SafBP with
high affinity. Hickey and Krueger (1974) also found that corn
coleoptiles treated with alachlor had reduced lignification. Insofar as
lignification affects cell shape and tissue structure, perturbation of
this process by the herbicides and/or safeners could account for some
of the observed cytological and morphological effects of the herbicides
(Ebert, 1980). However, SafBP does not catalyze methyl transfer from
S-adenosyl Met to catechol or caffeic acid. SafBP might
catalyze methyl transfer to an as-yet-unknown substrate such as a
flavonoid, it might require special conditions (e.g. pH, cofactors, or
metal ions) not present in our assays, or it might not actually be an
OMT. The absence of an amino acid motif that is highly conserved among
all known OMTs suggests that SafBP is not an enzymatically active OMT
(Kagan and Clarke, 1994).
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FOOTNOTES |
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Received September 17, 1997;
accepted November 20, 1997.
The accession number for the SBP1 sequence described in
this article is AF033496.
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ABBREVIATIONS |
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Abbreviations:
EPTC, S-ethyl
dipropylthiocarbamate.
IC50, inhibitor concentration that
reduces specific binding by 50%.
IPTG, isopropyl-
-d-thiogalactopyranoside.
OMT, O-methyltransferase.
Saf, the dichloroacetamide safener
(R,S)-3-dichloroacetyl-2,2,5-trimethyloxazolidine
(also known as R-29148) .
SafBA, safener-binding activity.
SafBP, safener-binding protein.
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ACKNOWLEDGMENTS |
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We thank Benjamin Burr (Brookhaven National Laboratory, Upton, NY), Richard Kneusel (University of Freiburg, Germany), Maurice Snook (U.S. Department of Agriculture, Athens, GA), Scott Chilton (North Carolina State University, Raleigh), and Tim Helantjaris (Pioneer Hi-Bred International, Johnston, IA) for their generous gifts of biological and chemical materials. We thank Joe Leykam of the Michigan State University Macromolecular Structure Facility for proteolytic digestion, sequencing of SafBP peptides, and oligonucleotide synthesis.
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LITERATURE CITED |
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Top
Abstract
Introduction
Methods
Results
Discussion
References
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