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Plant Physiol. (1999) 119: 481-488 Complementary DNA Cloning and Characterization of Ferredoxin Localized in Bundle-Sheath Cells of Maize Leaves1
Division of Enzymology (T.M., Y.K.-A., T.H.), and Division of Organic Chemistry (H.M., T.T., Y.S.), Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871 Japan; and Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871 JapanDepartment of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601 Japan (H.S., T.S.)
In
maize (Zea mays L.) two leaf-specific ferredoxin (Fd)
isoproteins, Fd I and Fd II, are distributed differentially in
mesophyll and bundle-sheath cells. A novel cDNA encoding the precursor
of Fd II (pFD2) was isolated by heterologous hybridization using a cDNA
for Fd I (pFD1) as a probe. The assignment of the cDNAs to the Fds was
verified by capillary liquid-chromatography/electrospray ionization-mass spectrometry. RNA-blot analysis demonstrated that transcripts for Fd I and Fd II accumulated specifically in mesophyll and bundle-sheath cells, respectively. The mature regions of pFD1 and
pFD2 were expressed in Escherichia coli as functional
Fds. Fd I and Fd II had similar redox potentials of
Maize (Zea mays L.), a typical C4
plant, is characterized by the compartmentation of carbon assimilation
into two differentiated photosynthetic cells, MC and BSC. Atmospheric
CO2 is first incorporated into oxaloacetate in
the MC cytosol and is successively reduced to malate with the
consumption of NADPH in the MC chloroplasts (Hatch, 1987 Some other NAD(P)H-requiring processes are also restricted to MC in
maize leaves. The reduction of nitrate occurs exclusively in MC (Moore
and Black, 1979 On the other hand, BSC chloroplasts produce ATP required to drive the
C3 cycle by cyclic electron flow via PSI,
irrespective of the absence of PSII (Edwards and Walker, 1983 Fd, an electron-transfer protein, occupies a key position both for
transferring the photoreducing power to FNR, hence the formation of
NADPH, and for mediating the cyclic electron flow around PSI (Arnon,
1989 Fd is present as isoforms in most of the higher plants examined to
date. In maize four Fd isoproteins (Fd I to Fd IV) were found in young
seedlings (Kimata and Hase, 1989 We previously obtained a cDNA for Fd I from a cDNA library of maize
leaves (Hase et al., 1991a Plant Materials
Purification of Fd Isoproteins from Maize Leaves About 250 g of leaf tissue was homogenized with a Waring blender in 1 L of an ice-cold extraction buffer (50 mM Tris-HCl, pH 7.5, 100 mM NaCl, 0.5 mM EDTA, 0.5% [v/v] 2-mercaptoethanol, and 1 mM PMSF) containing 10% (w/v) Polyclar AT. The homogenate was filtered through two layers of Miracloth (Calbiochem). The leaf debris were ground further in a mortar with a pestle in a small volume of extraction buffer containing quartz sand. The combined filtrate was centrifuged at 10,000g for 10 min at 4°C. The supernatant was fractionated by the addition of ammonium sulfate to 70% saturation, and the resulting precipitated material was removed by centrifugation at 12,000g for 10 min. The supernatant containing Fd isoproteins was passed through a small DE-52 column (Whatman), and absorbed proteins were eluted with 50 mM Tris-HCl, pH 7.5, and 700 mM NaCl. Fd isoproteins were isolated by successive chromatography on a Sephadex G-75 column (Pharmacia), a DE-52 column, and a Phenyl-Superose column (Pharmacia) as described previously (Hase et al., 1991a ; Matsumura et al., 1997).
Screening of a cDNA Library, Subcloning, and Sequencing A cDNA library, constructed in pUEX1 vector (Amersham) with poly(A+) RNA prepared from maize seedlings (Sakakibara et al., 1991), was screened by colony hybridization (Sambrook et al.,
1989) with full-length pFD1 cDNA (Hase et al., 1991a) as a probe.
Positive clones were further screened with the 3 UTR of pFD1 to
distinguish clones for Fd I from clones for other Fd isoproteins. The
probes were labeled by random priming (Feinberg and Vogelstein, 1984) in the presence of [ -32P]dCTP. The probed
filters were washed under low-stringency conditions in 2× SSC (300 mM NaCl and 30 mM sodium
citrate, pH 7.0) and 0.1% (w/v) SDS at 42°C
for the first screening and under high-stringency conditions in 0.1×
SSC (15 mM NaCl and 1.5 mM sodium citrate, pH
7.0) and 0.1% (w/v) SDS at 50°C for the second screening. The filters were then subjected to autoradiography.
Extraction of RNA and Blot Analysis Total RNAs from whole leaves, MC protoplasts, and BSC strands were prepared as described previously (Sakakibara et al., 1995). Total RNA
(10 µg) was separated by electrophoresis on a 1% (w/v) agarose gel
containing 6.3% (v/v) formaldehyde (Sambrook et al., 1989) and blotted
onto nylon membranes (Hybond-N+, Amersham). The
blots were probed with various cDNA fragments that had been labeled
with [-32P]dCTP. Hybridization and washing
of the filters were performed as described previously (Hase et al.,
1991a).
Reduction and Carboxymethylation of Fd I and Fd II and Analysis of
Proteolytic Fragments by Capillary LC/ESI-MS
Construction of Expression Plasmids of Fd I and Fd II and Site-Directed Mutagenesis The pTrc99A expression vector (Pharmacia) was digested with PstI and HindIII, end-filled with Klenow fragment, and self-ligated to delete the PstI site in the polylinker region. The resulting vector, pTrc99A-1, was used for the construction of the expression plasmids for Fd I and Fd II. A pair of primers, ATTACCATGGCCACCTACAACGTGAAGCTGA and ATTATGCATGCTTACATGAACAGTGCT, was used to amplify a DNA fragment containing the mature region of pFD1. The PCR fragment was digested with SphI, end-filled with Klenow fragment, digested with NcoI, and inserted into the NcoI/SmaI site of pTrc99A-1 to construct the Fd I expression plasmid pTMmFD1. A unique PstI site was present at the same position of pFD1 and pFD2, and the amino acid sequences of Fd I and Fd II were identical in the region from the N terminus to the residue corresponding to the PstI site. Thus, a DNA fragment from the PstI site to an NheI site in the 3 UTR of pFD2 was replaced with
the PstI/XbaI fragment of pTMmFD1 to obtain the
Fd II expression plasmid pTMmFD2. We also altered the codon usage of
amino acids near the translation start site of pTMmFD1 and pTMmFD2 to
obtain higher expression efficiency.
Expression and Purification of Recombinant Fd Isoproteins Escherichia coli JM105 cells were transformed with the expression plasmids for Fd I or Fd II. The transformants were grown overnight at 37°C in Luria-Bertani medium containing 50 µg/mL ampicillin. The seed cultures were inoculated into 8 L of the same medium at 1% volume. The cells were grown at 37°C with vigorous aeration for 2 h. Then, isopropyl- -D( )-thiogalactopyranoside was added to a
final concentration of 0.5 mM. After further
cultivation for 8 to 12 h, the cells were collected by
centrifugation at 5,000g for 10 min and stored at
30°C. The frozen cells were suspended in 50 mM Tris-HCl, pH 7.5, containing 25% (w/v) Suc,
0.5% (v/v) 2-mercaptoethanol, and 0.5 mM PMSF
and treated with lysozyme at a concentration of 0.5 mg/mL on ice for
about 10 min. The cell suspension was diluted 2-fold with 50 mM Tris-HCl, pH 7.5, 60 mM
NaCl, and 3 mM EDTA, and then 30°C acetone
was added at a final concentration of 40% (v/v). The resulting
homogenate was centrifuged at 10,000g for 10 min. The
supernatant was passed through a DEAE-cellulose column, and the
absorbed Fd proteins were eluted with 50 mM
Tris-HCl, pH 7.5, 700 mM NaCl. Further purification of Fd isoproteins was carried out as described above.
Measurement of Oxidation-Reduction Potentials of Fds Oxidation-reduction potentials of Fd I and Fd II were measured by cyclic voltammetry using an In2O3 electrode modified with poly-L-Lys as described previously (Taniguchi et al., 1997).
Assay for Electron-Transfer Activity Electron-transfer activity of Fd was assayed by measuring the rate of Cyt c reduction, as described previously (Hase et al., 1991b). The reaction mixture contained (in a total volume of 800 µL)
0.5 mM NADPH, 40 nM FNR,
0.2 mM Cyt c, 50 mM Tris-HCl (pH 7.5), and 100 mM NaCl. The reaction was initiated by the
addition of Fd at final concentrations from 5 to 100 µM. Cyt c reduction was measured by
monitoring the increase in A550.
Cloning and Characterization of cDNAs for Fd Isoproteins in Maize Leaves Fd I and Fd II have the same N-terminal sequences up to residue 19 (Hase et al., 1991a), and antibodies raised against Fd I cross-reacted
with Fd II (Kimata and Hase, 1989), indicating a close sequence
similarity between the two Fds. A cDNA, pFD1, encoding a precursor of
Fd I was previously isolated (Fig. 1A; Hase et al., 1991a). To obtain a cDNA clone for Fd II, a cDNA library
prepared from maize leaves was screened by heterologous hybridization
with a combination of the entire region and the 3 UTR fragment of pFD1
as the probes. Twenty positive clones were obtained from 5 × 104 colonies by hybridization with the
full-length cDNA. Six of these clones, which did not hybridize with the
3 UTR fragment, were selected as candidates for clones encoding Fd II.
The 5 and 3 terminal sequences of the six clones were determined.
Four encoded the same Fd polypeptide, whose C-terminal Leu residue
agreed with that of Fd II. In the remaining two clones, one was the
same clone as pFD5 previously reported (Hase et al., 1991a; accession
no. M73828) and the other was an unidentified new clone for Fd.
MS Analysis of Fd I and Fd II The assignment of pFD1 and pFD2 as the genes for Fd I and Fd II, respectively, was made based only on the terminal sequences of the two Fds. To obtain further structural information about Fd I and Fd II, we carried out MS. Fd I and Fd II purified from maize leaves (Fig. 2A) were reduced and carboxymethylated. They were then digested with lysylendopeptidase and subjected to capillary LC/ESI-MS. The digests of both Fds were separated into three major peaks (Fig. 2B) and their Mrs were measured. Lysylendopeptidase cleaves the polypeptide bond at the C-terminal side of Lys. Thus, the determined Mrs of each of the three peptides derived from Fd I and Fd II could be equated to those of the segments of the deduced amino acid sequences of pFD1 and pFD2, as shown in Table I. We concluded that pFD1 and pFD2 encoded Fd I and Fd II, respectively.
Cell-Specific Expression of Fd I and Fd II in Maize Leaves To investigate the expression of Fd I and Fd II genes in MC and BSC in leaves, total RNAs were isolated from whole leaves, MC, and BSC. RNA-blot analysis was performed using the restriction fragments at the 3 UTR of pFD1 and pFD2 as gene-specific probes (Fig. 1A). cDNAs for
PEPC and the Rubisco small subunit were used as the marker probes for
MC and BSC, respectively. As shown in Figure
3, the transcripts of the two Fd genes
accumulated differently in the two types of photosynthetic cells. The
probes for pFD1 and pFD2 hybridized almost exclusively with the RNA
from MC and BSC, respectively.
Expression of Fd I and Fd II cDNAs in E. coli We first developed a large-scale expression system for the Fds in E. coli (Fig. 4). The mature region of pFD1 was amplified by PCR using a pair of primers with concomitant creation of the initiation Met codon at the N terminus. This fragment was inserted under the control of the trc promoter of pTrc99A-1 to yield pTMmFD1. Next, the third nucleotides (mostly C or G) within the first 11 codons were substituted synonymously with A or T to give pTMmFD1-1. These changes in codon usage might reduce the secondary structure within the mRNA around the translation start site, thereby increasing translation efficiency in E. coli (De Boer and Hui, 1990). Figure 5 shows an overexpression of the Fd I
polypeptide. Yields of Fd I with pTMmFD1 and pTMmFD1-1 were about 0.2 and 10 mg, respectively, from 1 L of bacterial culture.
Electron-Transfer Ability of Fd I and Fd II Fd I and Fd II were purified from the recombinant E. coli as functional molecules with a [2Fe-2S] cluster. The recombinant Fds were indistinguishable from the authentic Fds in maize leaves in terms of their absorption spectra and mobilities on nondenaturing PAGE (data not shown). Redox potentials of Fd I and Fd II were determined to be423 and 406 mV, respectively, by cyclic
voltammetry. These values were within the range of those reported for
various photosynthetic Fds from plants and algae (Cammack et al.,
1977). The electron-transfer abilities of Fd I and Fd II were assayed in a reconstitution system of Cyt c reduction by FNR (Fig.
6). Fd I showed higher electron-transfer
activity than Fd II at all Fd concentrations examined. This was mainly
due to the difference in the affinity of FNR to the Fds. The
Km was about 3 times higher for Fd II than
for Fd I, whereas Vmax did not show a large
difference between the two Fds (Table
II).
We have isolated and characterized two maize Fd cDNAs,
pFD1 and pFD2, the transcripts of which specifically accumulated in MC
and BSC, respectively. From the analysis of the purified Fds by MS, we
concluded that pFD1 and pFD2 encoded the precursors of Fd I and Fd II,
respectively. Previous analysis with nondenaturing PAGE indicated that
Fd I was distributed in the chloroplasts of both MC and BSC, whereas Fd
II was localized only in the chloroplasts of BSC (Kimata and Hase,
1989
2 Present address: Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo, 113-8602 Japan. * Corresponding author; e-mail a-yoko{at}protein.osaka-u.ac.jp; fax 81-6-879-8613. Received August 27, 1998;
accepted November 2, 1998.
Abbreviations: BSC, bundle-sheath cell(s). ESI, electrospray ionization. FNR, Fd-NADP+ oxidoreductase. LC, liquid chromatography. MC, mesophyll cell(s). PEPC, PEP carboxylase. UTR, untranslated region.
We thank Professor Isao Taniguchi (Department of Applied Chemistry and Biochemistry, Faculty of Engineering, Kumamoto University, Japan) for measuring the redox potentials of Fds. The accession number for the nucleotide sequence data reported in this paper is AB016810.
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Abstract
Introduction
