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lnJonesion version

Nitrate uptake and reduction


Nitrate and ammonium transport



Sistem penyerapan nitrat tumbuhan tinggi terdiri dari suatu sistem, transportasi konstitutiI
aIinitas rendah (Lats) (mungkin sebuah sistem carrier atau saluran anion), dan diinduksi
dengan, aIinitas tinggi sistem transportasi (HATS) diatur dengan pasokan energi sel, dan
intraseluler nitrat konsumsi, dan yang aktivitasnya tergantung pada gradien elektrokimia
proton. Sistem yang terakhir ini dianggap sebagai mekanisme H

/ anion co-operator
transportasi yang menghasilkan depolarisasi plasmamembrane transien pada penambahan
nitrat. Depolarisasi ini menetral oleh plasmamembrane H

-ATPase. Membran plasma proton


ATP-ase yang disebabkan oleh nitrat. Selain sistem penyerapan nitrat, tanaman memiliki
sistem diinduksi nitrat penghabisan, membutuhkan baik RNA dan sintesis protein. Sistem
penghabisan, bagaimanapun, memiliki tingkat turnover lebih lambat daripada sistem
penyerapan. Nitrit juga diangkut oleh dua sistem, dimana sistem aIinitas rendah-mungkin
memainkan peran yang lebih besar daripada di serapan nitrat. Dalam beberapa, tapi tidak
dalam semua kasus, sistem tinggi aIinitas telah ditunjukkan identik dengan transportasi nitrat,
dengan studi persaingan penyerapan serta perubahan tegangan.
erakan nitrit dari sitosol ke kloroplas muncul untuk melibatkan transportasi proton-link dari
nitrit. erakan cepat HNO
2
di amplop kloroplas dalam akan memerlukan beberapa
transportasi proton aktiI dari stroma ke dalam ruang eksternal. Kehadiran H

-ATPase pada
amplop kloroplas batin yang memompa H

keluar dari stroma ke sitosol dapat memenuhi
peran ini. Ion amonium yang diambil oleh saturable, tapi rupanya konstitutiI, operator sistem
dengan aIinitas substrat yang tinggi, yang dapat melakukan uniport amonium selama H

-
ATPase mengembalikan Em. Rendah aIinitas komponen transportasi dirangsang oleh pH
eksternal tinggi dan mungkin mencerminkan diIusi NH
3
bermuatan di Iase lipid
plasmalemma tersebut. Kedua aIinitas tinggi dan sistem transportasi rendah aIinitas amonium
tampaknya konstitutiI. Dalam akar Km beras untuk penyerapan amonium adalah sekitar 32
um. Sebuah induksi transien dari sistem transportasi amonium (meningkat Vmax) terjadi
pada paparan bibit beras untuk kekurangan oksigen, hal ini dapat terjadi sebagai respon
terhadap hipoksia akibat asidosis sitoplasma. Tiga pengangkut amonium telah diidentiIikasi
dalam akar Arabidopsis, konstitutiI, diurnally diatur, dan kelaparan-diinduksi.
Jika amonium memasuki sel pada tingkat tinggi, hal itu menyebabkan depolarisasi membran
yang kuat dan akan memblokir anion / H

co-transport. Ini mungkin mekanisme utama yang
menghambat penyerapan ion amonium nitrat. Atau persaingan antara sistem serapan nitrat
dan glutamin sintetase (S) untuk ATP dapat di account bagian untuk penghambatan
amonium nitrat serapan (terjadi hanya ketika S aktiI). Butz dan Jackson (1977)
mengusulkan bahwa reduktase nitrat (NR) dimer yang membentang membran unit, ditambah
dengan ATP-ase, bertanggung jawab untuk kedua transportasi nitrat dan pengurangan.
Antibodi terhadap nitrat reduktase Chlorella mendeteksi protein dalam membran plasma akar
barley, dan Ig Iragmen antibodi ini menghambat transportasi nitrat oleh akar jelai.
Membran plasma reduktase nitrat merupakan sebagian kecil dari nitrat reduktase total, ia
memiliki berat molekul lebih rendah daripada bentuk sitosolik enzim, dan tidak muncul untuk
mewakili transporter diinduksi nitrat reduktase nitrat atau diinduksi; perannya saat ini tidak
jelas.
Warner dan HuIIaker (1989) menyangkal hubungan antara NR dan transportasi nitrat.
enotipe jelai kurang baik NADH-spesiIik dan NAD (P) H-NRS menunjukkan kinetika
serapan nitrat yang sama sebagai wildtype (Warner dan HuIIaker, 1989). Namun, dalam NR-
kekurangan mutan masih ada jejak aktivitas NR yang bisa saja karena bentuk membran
plasma berat molekul rendah dari enzim didalilkan untuk terlibat dalam transportasi nitrat.
Sebuah mutan dari Arabidopsis (chl1) yang tahan terhadap klorat ditemukan bahwa sebagian
cacat dalam penyerapan nitrat. en CHL1 adalah klon dari garis T-DNA-tagged
diidentiIikasi oleh Ken Feldmann. en ini mengkode protein hidroIobik dengan 12 segmen
membran mencakup aktivitas nitrat yang memberikan transportasi ke oosit Xenopus. en
CHL1 dinyatakan terutama di akar dan disebabkan oleh nitrat dan pH rendah. Protein CHL1
tampaknya menjadi transporter aIinitas nitrat / klorat rendah. Sebuah alel baru chl1
ditemukan dalam garis dari Arabidopsis membawa elemen Ac aktiI. Mutan ini memiliki
penyisipan di 4 intron gen CHL1. Penyisipan itu terbukti menjadi elemen, aktiI transposabel
endogen, yang bernama tag1. Touraine dan lass (1997) menunjukkan bahwa dalam
pengambilan mutan chl1-5 penghapusan nitrat terganggu hanya ketika tanaman ditanam di
amonium nitrat; penyerapan nitrat tidak terganggu ketika KNO
3
adalah sumber N tunggal.
Namun serapan klorat secara signiIikan lebih rendah daripada di wildtype ketika tumbuh di
KNO
3
. Touraine dan lass (1997) menunjukkan bahwa aIinitas kedua sistem transportasi
rendah (Lats) mampu mengkompensasi kekurangan chl1-5 di KNO
3
-tumbuh tanaman;
pertumbuhan pada NH
4
NO
3
dapat down-mengatur Lats kedua cukup bahwa perbedaan
diantisipasi dalam nitrat serapan menjadi jelas. Seperti Ulasan terakhir dengan Chrispeels et
al (1999), CHL1 juga dapat berkontribusi untuk kedua diinduksi dan sistem konstitutiI nitrat
tinggi aIinitas transportasi saat amonium hadir dan / atau pH rendah. Jadi, selain menjadi
transporter aIinitas rendah nitrat, CHL1 juga terlibat dalam kedua diinduksi dan Iase
konstitutiI tinggi aIinitas serapan nitrat dalam Arabidopsis (Liu et al, 1999). CHL1 adalah
anggota dari keluarga NRT1 transporter nitrat. Anggota keluarga NRT2 adalah transporter
nitrat tinggi aIinitas, akar tertentu, nitrat dan amonium diinduksi / direpresi glutamin. Dua
mutasi telah ditemukan dalam gen (NRT2) dari Arabidopsis thaliana yang secara khusus
mengganggu konstitutiI, tinggi aIinitas serapan nitrat. Mutan ini dipilih untuk ketahanan
terhadap 0,1 mM klorat dengan tidak adanya nitrat.
Bukti bahwa Arabidopsis CHL1 (AtNRT1) gen mengkodekan komponen diinduksi aIinitas
rendah serapan nitrat, telah mengharuskan "dua-komponen" model untuk memperhitungkan
konstitutiI aIinitas rendah serapan. Para homolog CHL1, AtNRT1: 2 (awalnya bernama
NTL1) mengkodekan komponen konstitutiI aIinitas rendah serapan nitrat. Sebuah homolog
beras dari CHL1 Arabidopsis (AtNRT1) protein, OsNRT1, telah diidentiIikasi (Lin et al,
2000). Berbeda dengan kegiatan dual-aIinitas nitrat transportasi CHL1, OsNRT1 hanya
ditampilkan aIinitas rendah transportasi nitrat |Km 9 mM| Aktivitas pada oosit Xenopus.
OsNRT1 adalah konstitutiI dinyatakan dalam lapisan paling luar rambut akar, epidermis dan
akar, dan mengkodekan komponen konstitutiI dari sistem aIinitas rendah nitrat serapan beras.
Lejay et al (1999) telah meneliti akar serapan nitrat dan ekspresi dua gen transporter akar
nitrat (Nrt2; 1 dan Nrt1) dalam menanggapi perubahan di N-atau C-status hidroponik tumbuh
tanaman Arabidopsis thaliana. Ekspresi Nrt2; 1 adalah up-diatur oleh kelaparan nitrat dalam
tipe liar tanaman dan oleh N-pembatasan dalam nitrat reduktase (NR) mutan kekurangan
ditransIer ke nitrat sebagai sumber N tunggal (Lejay et al, 1999). Jadi, ekspresi Nrt2; 1 berada
di bawah represi umpan balik oleh N-metabolit yang dihasilkan dari reduksi nitrat. Ekspresi
Nrt1 tidak dikenakan seperti represi sebuah. Namun, Nrt1 selesai-dinyatakan dalam mutan
NR bahkan di bawah kondisi yang cukup N-(pertumbuhan pada media NH4NO3),
menunjukkan bahwa ekspresi gen ini dipengaruhi oleh adanya NR aktiI, tetapi tidak oleh N-
status tanaman.
Sebuah Iull-length cDNA, mNRT2, pengkodean transporter aIinitas tinggi nitrat diduga
telah diisolasi dari sebuah perpustakaan cDNA lycine max akar. Protein mNRT2
disimpulkan adalah 530 asam amino panjang dan mengandung 12 membran-mencakup
diduga domain dan panjang, hidroIilik C-terminal domain (Amarasinghe et al, 1998).
mNRT2 terkait dengan transporter aIinitas tinggi nitrat dalam eukariota Chlamydomonas
reinhardtii dan Aspergillus nidulans, dan putatiI tinggi aIinitas transporter nitrat dalam barley
dan tembakau (Amarasinghe et al, 1998). mNRT2 tingkat mRNA yang hampir tidak
terdeteksi dalam amonium-tumbuh tanaman, tinggi dalam nitrogen-kekurangan tanaman, dan
tertinggi di nitrat tumbuh tanaman (Amarasinghe et al, 1998). Dalam Nicotiana
plumbaginiIolia gen NpNRT2.1 mengkodekan komponen diinduksi putatiI dari sistem
penyerapan tinggi aIinitas nitrat. Amonium, atau metabolit hilir lebih lanjut, dapat
menimbulkan eIek yang represiI pada masuknya nitrat baik di tingkat transkripsi dan pasca-
transkripsi.
Dalam angiosperma kelautan Zostera marina nitrat (hadir pada konsentrasi mikromolar dalam
air laut) diserap terhadap perbedaan potensial elektrokimia yang curam menyeberangi
membran plasma melalui sistem tinggi aIinitas Na -symport. Para nrtP gen dan narB
mengkodekan nitrat / nitrit reduktase nitrat permease dan masing-masing, di laut
cyanobacterium Synechococcus sp. regangan PCC 7002. NrtP adalah anggota dari
superIamili Iasilitator utama dan tidak berhubungan dengan mengikat ATP-kaset-jenis
transporter nitrat dijelaskan untuk air tawar strain cyanobacteria. Namun, NrtP ini mirip
dengan tipe transporter NRT2 nitrat ditemukan dalam organisme beragam.

riqinol version
Nitrate uptake and reduction
Nitrate and ammonium transport



The nitrate uptake system oI higher plants consists oI a constitutive, low aIIinity transport
system (LATS) (possibly a carrier system or an anion channel), and an inducible, high
aIIinity transport system (HATS) regulated by cellular energy supply, and by intracellular
nitrate consumption, and whose activity depends on the proton electrochemical gradient. The
latter system is regarded as an H

/anion co-transport carrier mechanism that produces


transient plasmamembrane depolarization upon addition oI nitrate. The depolarization is
counteracted by the plasmamembrane H

-ATPase. The plasma membrane proton ATP-ase is


induced by nitrate. In addition to the nitrate uptake system, plants have an inducible nitrate
eIIlux system, requiring both RNA and protein synthesis. The eIIlux system, however, has a
much slower turnover rate than the uptake system. Nitrite is also transported by two systems,
oI which the low-aIIinity system may play a greater role than in nitrate uptake. In some, but
not in all cases, the high-aIIinity system has been shown to be identical with that oI nitrate
transport, by uptake competition studies as well as voltage changes.
Movement oI nitrite Irom the cytosol to the chloroplast appears to involve a proton-linked
transport oI nitrite. The rapid movement oI HNO
2
across the chloroplast inner envelope
would require some active proton transport Irom the stroma into the external space. The
presence oI an H

-ATPase on the chloroplast inner envelope which pumps H

out oI the
stroma into the cytosol may IulIill this role. Ammonium ions are taken up by a saturable, but
apparently constitutive, carrier system with high substrate aIIinity, which may carry out
ammonium uniport as long as H

-ATPases restore Em. The low-aIIinity component oI


transport is stimulated by high external pH and probably reIlects diIIusion oI uncharged NH
3

across the lipid phase oI the plasmalemma. Both the high aIIinity and low aIIinity ammonium
transport systems appear to be constitutive. In rice roots the K
m
Ior ammonium uptake is
about 32 uM. A transient induction oI the ammonium transport system (increased V
max
)
occurs upon exposure oI rice seedlings to oxygen deprivation; this may occur in response to
hypoxia-induced cytoplasmic acidosis. Three ammonium transporters have been identiIied in
Arabidopsis roots; constitutive, diurnally regulated, and starvation-induced.
II ammonium enters the cell at high rates, it causes strong membrane depolarization and will
block anion/H

co-transport. This may be the primary mechanism by which ammonium ions


inhibit nitrate uptake. Alternatively competition between the nitrate uptake system and
glutamine synthetase (S) Ior ATP may in part account Ior ammonium inhibition oI nitrate
uptake (occurs only when S is active). Butz and Jackson (1977) proposed that a nitrate
reductase (NR) dimer that spans a unit membrane, plus an ATP-ase, is responsible Ior both
nitrate transport and reduction. Antibodies against Chlorella nitrate reductase detect a protein
in the plasma membrane oI barley roots, and Ig Iragments oI these antibodies inhibited
nitrate transport by barley roots. The plasma membrane nitrate reductase represents a small
Iraction oI the total nitrate reductase, it has a much low molecular weight than the cytosolic
Iorm oI the enzyme, and does not appear to represent the inducible nitrate transporter or the
inducible nitrate reductase; its role is presently unclear.
Warner and HuIIaker (1989) deny a connection between NR and nitrate transport. enotypes
oI barley lacking both the NADH-speciIic and NAD(P)H-NRs show the same kinetics oI
nitrate uptake as the wildtype (Warner and HuIIaker, 1989). However, in these NR-deIicient
mutants there was still a trace oI NR activity which could have been due to the low molecular
weight plasma membrane Iorm oI the enzyme postulated to be involved in nitrate transport. A
mutant oI Arabidopsis (chl1) that is resistant to chlorate was Iound that is partially deIective
in nitrate uptake. The CHL1 gene was cloned Irom a T-DNA-tagged line identiIied by Ken
Feldmann. This gene encodes a hydrophobic protein with 12 membrane spanning segments
that conIers nitrate transport activity to Xenopus oocytes. The CHL1 gene is expressed
primarily in roots and is induced by nitrate and low pH. The CHL1 protein appears to be a
low aIIinity nitrate/chlorate transporter.
A new allele oI chl1 was discovered in a line oI Arabidopsis carrying an active Ac element.
This mutant had an insertion in the 4
th
intron oI the CHL1 gene. The insertion was shown to
be an active, endogenous transposable element, which was named Tag1. Touraine and lass
(1997) show that in chl1-5 deletion mutants nitrate uptake is impaired only when plants are
grown on ammonium nitrate; nitrate uptake is not impaired when KNO
3
is the sole N source.
However chlorate uptake was signiIicantly lower than in wildtype when grown on KNO
3
.
Touraine and lass (1997) suggest that a second low aIIinity transport system (LATS) is able
to compensate Ior the chl1-5 deIiciency in KNO
3
-grown plants; growth on NH
4
NO
3
may
down-regulate the second LATS enough that the anticipated diIIerence in nitrate uptake
becomes apparent. As reviewed recently by Chrispeels et al (1999), CHL1 may also
contribute to both the inducible and constitutive high-aIIinity nitrate transport systems when
ammonium is present and/or the pH is low. Thus, in addition to being a low-aIIinity nitrate
transporter, CHL1 is also involved in both the inducible and constitutive phases oI high-
aIIinity nitrate uptake in Arabidopsis (Liu et al, 1999). CHL1 is a member oI the NRT1 Iamily
oI nitrate transporters. Members oI the NRT2 Iamily are high-aIIinity nitrate transporters, root
speciIic, nitrate inducible and ammonium/glutamine repressible. Two mutations have been
Iound in a gene (NRT2) oI Arabidopsis thaliana that speciIically impair constitutive, high-
aIIinity nitrate uptake. These mutants were selected Ior resistance to 0.1 mM chlorate in the
absence oI nitrate.
The evidence that Arabidopsis CHL1 (AtNRT1) gene encodes an inducible component oI
low-aIIinity nitrate uptake, has necessitated a "two-component" model to account Ior
constitutive low-aIIinity uptake. The CHL1 homolog, AtNRT1.2 (originally named NTL1)
encodes a constitutive component oI low-aIIinity nitrate uptake. A rice homolog oI the
Arabidopsis CHL1 (AtNRT1) protein, OsNRT1, has been identiIied (Lin et al, 2000). In
contrast to the dual-aIIinity nitrate transport activity oI CHL1, OsNRT1 displayed only low-
aIIinity nitrate transport |Km 9 mM| activity in Xenopus oocytes. OsNRT1 is constitutively
expressed in the most external layer oI the root, epidermis and root hair, and encodes a
constitutive component oI a low-aIIinity nitrate uptake system in rice.
Lejay et al (1999) have examined root nitrate uptake and expression oI two root nitrate
transporter genes (Nrt2,1 and Nrt1) in response to changes in the N- or C-status oI
hydroponically grown Arabidopsis thaliana plants. Expression oI Nrt2,1 is up-regulated by
nitrate starvation in wild-type plants and by N-limitation in a nitrate reductase (NR) deIicient
mutant transIerred to nitrate as sole N source (Lejay et al, 1999). Thus, expression oI Nrt2,1
is under Ieedback repression by N-metabolites resulting Irom nitrate reduction. Expression oI
Nrt1 is not subject to such a repression. However, Nrt1 is over-expressed in the NR mutant
even under N-suIIicient conditions (growth on NH
4
NO
3
medium), suggesting that expression
oI this gene is aIIected by the presence oI active NR, but not by N-status oI the plant.
A Iull-length cDNA, mNRT2, encoding a putative high-aIIinity nitrate transporter has been
isolated Irom a Glycine max root cDNA library. The deduced mNRT2 protein is 530 amino
acids in length and contains 12 putative membrane-spanning domains and a long, hydrophilic
C-terminal domain (Amarasinghe et al, 1998). mNRT2 is related to high-aIIinity nitrate
transporters in the eukaryotes Chlamydomonas reinhardtii and Aspergillus nidulans, and to
putative high-aIIinity nitrate transporters in barley and tobacco (Amarasinghe et al, 1998).
mNRT2 mRNA levels were barely detectable in ammonium-grown plants, higher in
nitrogen-deprived plants, and highest in nitrate-grown plants (Amarasinghe et al, 1998). In
Nicotiana plumbaginifolia the NpNRT2.1 gene encodes a putative inducible component oI the
high-aIIinity nitrate uptake system. Ammonium, or a Iurther downstream metabolite, may
exert a repressive eIIect on nitrate inIlux at both transcriptional and post-transcriptional
levels.
In the marine angiosperm Zostera marina nitrate (present at micromolar concentrations in
seawater) is absorbed against a steep electrochemical potential diIIerence across the plasma
membrane via a high-aIIinity Na

-symport system. The genes nrtP and narB encode


nitrate/nitrite permease and nitrate reductase, respectively, in the marine cyanobacterium
Synechococcus sp. strain PCC 7002. NrtP is a member oI the major Iacilitator superIamily
and is unrelated to the ATP-binding cassette-type nitrate transporters described Ior Ireshwater
strains oI cyanobacteria. However, NrtP is similar to the NRT2-type nitrate transporters
Iound in diverse organisms.

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3
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3
-
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3
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3
-
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