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RI 
-Chain Gene Expression by GATA-1 Via Four GATA Motifs in the Promoter1
* Atopy (Allergy) Research Center, Juntendo University School of Medicine,
Biotechnology Research Center, University of Tokyo, and
Department of Molecular Cell Immunology and Allergology, Advanced Medical Research, Nihon University School of Medicine, Tokyo, Japan
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Abstract |
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 Top Abstract IntroductionMaterials and MethodsResultsDiscussionReferences |
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-chain, a subunit of two related multisubunit receptor
complexes, the Fc
RI and Fc
RIII, amplifies the mast cell response
and is necessary for the cell surface expression of FcRI in mouse.
The transient reporter assay indicated that -69/+4 region is required
for cell type-specific transcriptional regulation of mouse -chain
gene. EMSA using Abs against transcription factors or competitive
oligonucleotides demonstrated that -58/-40 region (containing
overlapping three GATA-1 sites, -53/-48, -46/-51, and -42/-47)
and -31/-26 region (containing one GATA-1 site) are recognized by
GATA-1. The promoter activity of -chain was decreased by nucleotide
replacements of the GATA-1 sites in mouse mast cell line PT18.
Furthermore, exogenously produced GATA-1 up-regulated the promoter
activity in CV-1 cells, which are negative in the -chain production
and the up-regulation was apparently suppressed by GATA-1 site
mutations. These results indicate that cell type-specific transcription
of mouse -chain gene is regulated by GATA-1. |
Introduction |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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RI is a member of the Ag receptor superfamily and composed of
-chain, -chain, and -chain (1). Binding of
allergen-IgE Ab complexes to the FcRI triggers the release of a
variety of chemical mediators from activated mast cells, which results
in allergic responses.
FcRI is functional in a form either of 2 or 2
complexes in human cells (2, 3). In human mast cells and
basophils that are positive -chain expression, functional FcRI is
actually expressed on the cell surface. However, in monocytes
(4), dendritic cells (5), Langerhans cells
(6), and eosinophils (7) that are negative in
-chain expression, FcRI is expressed on the surface even in the
absence of -chain. Thus, in human, -chain is not necessarily
required for cell surface expression of FcRI, whereas -chain is
known to facilitate the cell surface expression of the IgE receptor
(8). In contrast, the expression of mouse FcRI is
restricted on mast cells and basophils, suggesting that -chain is
completely required for cell surface expression of FcRI. All these
observations suggest that mouse -chain is a determinant of cell
type-specific expression of mouse FcRI. In addition, the -chain
is a key molecule in the allergic reaction because the -chain
amplifies signal from the immunoreceptor tyrosine-based activation
motif of the -chain (8). Therefore, elucidation
of the mechanisms for the mouse -chain expression could give us the
important information on the mast cells- and basophils-specific
transcriptional regulatory system.
In this report, we describe the analysis of transcriptional
regulatory elements for the mouse FcRI -chain gene expression by
luciferase reporter assay and EMSA, and demonstrate that GATA-1
transactivates -chain gene expression by recognizing repeating
GATA-1 motifs present in the promoter in a cell type-specific
manner.
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Materials and Methods |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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PT18 (mouse mast cell line), A20.2J (mouse B lymphoma cell line), RAW264.7 (mouse mono-macrophage cell line), and L5178Y (mouse lymphoma cell line) cells were cultured in RPMI 1640 medium (Sigma-Aldrich, St. Louis, MO) containing 10% FCS (Biological Industries, Haemek, Israel), 10 µM nonessential amino acid (Invitrogen, Leek, The Netherlands), 100 U/ml penicillin, and 100 µg/ml streptomycin. CV-1 (simian kidney cell line) cells were purchased from RIKEN Cell Bank (Tsukuba, Japan) and were cultured in DMEM medium (Sigma-Aldrich) containing 10% FCS, nonessential amino acids, penicillin, and streptomycin.
Plasmid construction
The mouse genomic DNA of FcRI -chain was prepared from
mouse genomic library and the transcription start site was
determined by 5'-RACE analysis (S. Hiraoka, M. Watanabe, Y.
Takagaki, K. Fujita-Suzuki, K. Okumura, and C. Ra, manuscript in
preparation; accession no. AB033617). The 2.4 kb of 5'-flanking region
was subcloned into BglII/NcoI site of reporter
plasmid pGL3-Basic (Promega, Madison, WI) and the resulting plasmid was
named -2.4k/pGL3-Basic. The plasmids containing a variety of
5'-deletion were constructed by an endonuclease/exonuclease III
deletion kit (TAKARA BIO, Otsu, Japan).
The plasmids in which several bases were replaced were constructed by site-directed mutagenesis using a Quick Change site-directed mutagenesis kit (Stratagene, La Jolla, CA). All mutations were verified by sequencing analysis.
The expression plasmid pCR-GATA-1 generated in our previous study (9, 10) was used to produce GATA-1.
Transfection and luciferase assay
Cells of 5 x 106 (PT18, A20.2J, RAW 264.7, and L5178Y) were transfected with 5 µg reporter plasmid and 25 ng pRL-CMV (Promega) by electroporation using Gene Pulsar II (Bio-Rad, Hercules, CA) set at 300 V and 950 µF. CV-1 cells of 1 x 106 were transfected with 500 ng reporter plasmid, 0.5 ng pRL-null (Promega), and 100 ng of pCR-GATA-1 expression plasmid or pCR3.1 empty plasmid (9, 10) by FuGENE 6 (Roche Diagnostics, Indianapolis, IN) according to the manufacturer’s instruction. The pRL-CMV and the pRL-null plasmids were used as the internal control of transfection efficiency.
After 20–24 h of cultivation, the cells were harvested and treated with a Dual-luciferase assay kit (Promega) for the measurement of luciferase activity. The luminescence was measured with Micro Lumat Plus (Berthold, Postfach, Germany).
EMSA
Probes for EMSA were prepared by annealing FITC-labeled
synthesized oligonucleotides. Each nucleotide sequence of sense strand
was shown as follows: probe-1,
5'-GGAGTCACTGATATCAATCAGCCTGGAGAC-3', and probe-2,
5'-CTGGAGACTTATCTGACAAGTAGGTTCCGCATGAAGATAATC-3' (Invitrogen). The
nonlabeled competitor oligonucleotides were prepared by a similar way.
The sequences of mutant competitors were shown in Fig. 3
A.
The sequences of sense strand of consensus oligonucleotides were as
follows: GATA, 5'-CACTTGATAACAGAAAGTGATAACTCT-3', and AP-1,
5'-CGCTTGATGACTCAGCCGGAA-3'.
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Nuclear extract of 5 µg was incubated with 5 pmol FITC-labeled probe for 20 min in the reaction buffer containing 500 ng poly(dI-dC), 1 mM MgCl2, 30 mM KCl, 10 mM HEPES (pH 7.9), 1 mM DTT, and 5% glycerol. The protein-DNA complexes were separated on a 4% polyacrylamide gel in 0.5 x TBE buffer (45 mM Tris-HCl, 32.3 mM boric acid, and 1.25 mM EDTA). For competition experiments, 50-fold molar excess of unlabeled competitor oligonucleotide were added to the binding reaction mixture. For inhibition experiments by Abs, 1 µg of Abs against GATA-1, GATA-2, GATA-3, and c-Jun purchased from Santa Cruz Biotechnology (Santa Cruz, CA) were used. All gels were subjected to fluorescence detector, Fluoroimager (Amersham Pharmacia Biotech, Uppsala, Sweden).
For in vitro transcription and translation, pCR-GATA-1 was used for the reaction using a TNT T7 Quick coupled transcription/translation system (Promega).
RT-PCR analysis
Detection of the mRNA for GATA-1 or G3PDH was performed by RT-PCR using 1 µg of total RNA prepared from each cell line using TRIzol Reagent (Invitrogen) as a template. For detection of GATA-1, the following primer set was used: 5'-ATGGATTTTCCTGGTCTAGGGGC-3' and 5'-TCAAGAACTGAGTGGGGCGATCACG-3', and a primer set to detect G3PDH was purchased from Clontech Laboratories (Palo Alto, CA).
Western blot analysis
Five micrograms of nuclear extract prepared from each cell line was subjected to Western blotting analysis. Anti-GATA-1 Ab, the same as that for EMSA analysis, was used as the primary Ab to detect GATA-1 protein. Anti-YY1 Ab, control rat IgG2a (control for anti-GATA-1 Ab), and control mouse IgG1 (control for anti-YY1 Ab) were purchased from Santa Cruz Biotechnology and were used as the primary Abs. Peroxidase-conjugated anti-rat IgG goat Abs (Wako Pure Chemical Industries, Osaka, Japan), or anti-mouse IgG sheep Abs (Santa Cruz Biotechnology) were used as the secondary Abs. Membrane was soaked with the ECL+plus Western blotting detection reagent (Amersham Pharmacia Biotech), and its chemiluminescence was detected by LAS-1000 plus (Fuji Film, Tokyo, Japan).
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Results |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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-chain promoter is activated in mast cell line
To examine the cell type specificity of the mouse FcRI
-chain promoter, we generated a reporter plasmid, -2.4k/pGL3-Basic,
by introducing 
2.4 kb 5'-upstream region of the putative
translational initiation codon of mouse -chain gene (-2357/+103) at
just upstream of the luciferase gene of promoterless plasmid
pGL3-Basic. The luciferase activity in the PT18 cells which were
transiently transfected with -2.4k/pGL3-Basic was 10-fold higher
than that from PT18 cells transfected with pGL3-Basic, whereas no
difference was observed between the luciferase activities directed by
-2.4k/pGL3-Basic and that of pGL3-Basic when the reporter plasmids
were introduced into FcRI -chain negative cell lines A20.2J,
L5178Y, or RAW264.7 (Fig. 1). This result
suggests that the -2357/+103 region principally contains all the
elements necessary for the expression and regulation of the promoter of
-chain which is active only in -chain positive cells.
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-chain
promoter region, several 5'-deletion constructs each carrying a portion
of 5'-flanking region from -2357 to +103 were generated and introduced
into PT18 cells (Fig. 2A). The
deletion of -2357/-117 region had no apparent effect on the promoter
activity. In contrast, the promoter activity was slightly decreased by
deletion of -116/-70, and markedly decreased by further deletion (see
-69/-33 and -32/+4). The luciferase activity directed by
+3/pGL3-Basic was reduced to the level which was equivalent to that of
pGL3-Basic. These results indicate that elements essential for
the activation of mouse -chain promoter are present between -69
and +4.
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-chain promoter are functional in
PT18 but not A20.2J, L5178Y, or RAW264.7, the deletion constructs
containing -69/+103, -32/+103, or +3/+103 of -chain gene were
introduced into each cell. As expected, all the constructs gave the
luciferase activity almost equal to that given by the empty plasmid in
A20.2J, L5178Y, and RAW264.7 (Figs. 1
and 2B). In contrast,
the distinct activity was observed when pGL3-Basic containing the
-chain promoter region -69/+103 or -32/+103 was introduced into
PT18 cells. We also found that the promoter activity directed by
-61/+4 was almost the same as that of -69/+4 in our similar
reporter assay (data not shown). From all these data, we assume that
-61/+4 contains elements essential for the activation of mouse
-chain promoter, which is activated in specific cells. GATA-1 binds to both of the regions -58/-38 and -31/-26
To identify the transcription factors binding the -61/+4 region,
EMSA was performed by using PT18 nuclear extract and FITC-labeled
probes in the presence or absence of the various competitive fragments.
The EMSA using probe-1 (-61/-32) gave several shifted bands (Fig. 3B). Among them, the shifted
band shown with an arrow was lost by addition of competitors -61,
-39, and -37. On the contrary, the shifted band apparently remained
even by addition of other competitors -58, -54, -52, -47, and -43
(Fig. 3B, lanes 5–9). This indicated that the
transcription factor responsible for this band shift recognized the
region -58/-38. Motif analysis using a program TFSEARCH
(http://www.cbrc.jp/research/db/TFSEARCH.html) revealed the presence of
three overlapping GATA-binding motifs in this region: two TGATAT and
one TGATTG (-53/-48, -46/-51, and -42/-47). The shifted band
shown with an arrowhead was apparently observed in the presence of
competitors -61 and -58, suggesting that the nuclear protein(s)
recognizing -61/-55 also presents in nuclear of PT18 cells. Other
shifted bands, shown with asterisks in Fig. 3B, lane
2, might be nonspecific because they disappeared equally by
addition of any competitors.
To confirm that GATA-1 is responsible for the band shift, similar EMSA
was performed in the presence of anti-GATA-1, GATA-2, GATA-3, or
c-Jun Abs, or oligonucleotides with GATA-1- or AP-1-recognition
sequence. The intensity of the shifted band marked with the arrow was
decreased by addition of anti-GATA-1 Ab or oligonucleotides with
GATA-1 consensus sequence (Fig. 4A, lanes 4 and
8), whereas Abs against GATA-2, 3, anti-c-Jun, and
oligonucleotide competitor with AP-1 consensus sequence had no effect
on this band (Fig. 4A, lanes 5, 6,
7, and 9). To confirm further the binding of
GATA-1 to this probe, GATA-1 was produced by in vitro
transcription/translation system and used for EMSA. Although several
shifted bands were seen, the shifted band that showed the mobility
identical with that seen with the nuclear protein from PT18 was
found (Fig. 4B). As expected, the band disappeared by
addition of anti-GATA-1 Ab (Fig. 4B). These results
indicate that the transcription factor GATA-1 binds probe-1.
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). Probe-2 (-39/+4 fragment) contains a
possible GATA motif (AGATAA) at -31/-26. The shifted band indicated
by an arrow disappeared by addition of Ab against GATA-1, but not by
Abs against GATA-2.
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-chain
promoter.
The -chain promoter is transactivated by GATA-1 via multiple
GATA-1 binding sites
To examine the contribution of the putative four GATA1-binding
sites to the promoter activity, we measured the luciferase activities
directed by the wild-type (-69/+103) and various altered promoters in
which nucleotide replacements were introduced at the four putative
GATA-binding sites by site-directed mutagenesis (Fig. 6A). The luciferase activity
directed by the mutant promoter M4 lacking a GATA-1 site at -31/-26
was apparently lower than that of the wild-type promoter (Fig. 6B). The mutant promoters (M12, M23, and M123) which lacked
two or three of GATA-1 sites in the region -53/-42 also gave lower
activities (Fig. 6B). When the additional mutation at
-31/-26 was introduced into M12 and M23, resulting promoters showed
further reduced activity (M124 and M234). The luciferase activity
directed by the mutant promoter M1234 lacking all of four GATA-1 motifs
was decreased to the level equivalent to that of promoterless plasmid
(pGL3-Basic). These results suggest that all four GATA-1-binding motifs
in -53/-26 are necessary for full transcriptional activity of
-chain promoter in mouse mast cells.
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-chain promoter
activity, the reporter plasmids constructed in this study were
cotransfected with pCR-GATA-1 expression plasmids or pCR3.1 empty
plasmid into CV-1 cells that do not express endogenous GATA-1 (Fig. 7). The -chain promoter was markedly
up-regulated 50-fold by the cotransfection of GATA-1 expression
plasmid when the reporter plasmid containing all the four GATA-1 motifs
(-69/+103 region) was used. The up-regulating effect of exogenously
expressed GATA-1 was apparently decreased when the fourth GATA-1 motif
(M4), or two of the other three GATA-1 motifs (-47/+103, -40/+103,
-32/+103, M12, and M23) was mutated. The altered promoters (+3/+103
and M1234) lacking all four GATA-1 gave further decreased level of
transactivation even by exogenous GATA-1. These results indicate that
GATA-1 actually transactivates the -chain promoter.
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-chain and
GATA-1
Above results indicated that GATA-1 transactivates the promoter of
-chain which is expressed in mast cells specifically. To confirm
cell type specificity of GATA-1 expression, we performed both RT-PCR
and Western blotting analysis. The transcript of GATA-1 was detected in
PT18 cells but not in A20.2J, L5178Y, and RAW264.7 (Fig. 8A). Similarly, we detected
GATA-1 protein in nuclear extract of PT18 by Western blotting analysis,
whereas no specific band corresponding to GATA-1 protein was observed
in other cell lines examined (Fig. 8B), which is in contrast
with the case of an ubiquitous transcription factor YY1 found in each
cell line (Fig. 8C). These results suggest that cell
type-specific expression of -chain is mediated by cell type-specific
expression of GATA-1.
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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-chain promoter is
functional only in PT18 mouse mast cell line, but not in monomacrophage
and lymphoma cell lines. By using a series of 5'-deletion promoter
constructs, the cell type-specific promoter was assigned within
-69/+103, although a slight decrease in the promoter activity was
observed by the deletion of -116/-70. This may suggest the presence
of additional cis-enhancing elements recognizing the deleted
region. Anyway, by EMSA using antitranscription factor Abs and various
competitive oligonucleotides, GATA-1 protein was identified to bind the
promoter region (-61/+3) of the -chain where three possible
GATA-1-binding (-53/-48, -46/-51, and -42/-47) and a single
possible GATA-1-binding site (-31/-26) are present. Furthermore,
reporter assay using PT18 cells (-chain+,
GATA-1+) and coexpression analysis using CV-1
cells (-chain-,
GATA-1-) indicated that those four GATA-1 sites
are required for full transcriptional activation by GATA-1 protein.
GATA-1 is abundantly expressed in mast cells (11) and
recognizes mast cell-specific cis-enhancing elements in
several genes such as FcRI -chain (9, 10),
carboxypeptidase A (12), IL-4 (13), and
chymase (14). In this study, expression of GATA-1 was
observed in PT18 cells (-chain positive), but not in other cell
lines examined (-chain negative) (Fig. 8). Therefore, GATA-1 is one
of the most probable candidates which regulate cell type-specific
expression of mouse -chain gene. When we performed coexpression
analysis in the cell lines L5178Y and RAW264.7
(-chain-/GATA-1-),
exogenously expressed GATA-1 had no positive effect on
-chain promoter activity (data not shown). This may be explained by
the possibility that PU.1, which is expressed in limited cells such as
lymphoid cells and monocyte/macrophages, may inhibit function of GATA-1
as reported by several studies (15, 16). Actually, we
found transcript of PU.1 in all cell lines used in Fig. 1, but not in
CV-1 (data not shown). Alternatively, an unknown transcription factor
that is involved in the transactivation of -chain promoter is absent
in these two cell lines.
Recently, -chain gene was found to be expressed in eosinophils in
human (17). It contrasts with the case of mouse or rat
where the expression of FcRI or -chain was not observed in
eosinophils, respectively (18, 19). These reports suggest
the different mechanisms for cell type-specific expression of -chain
between human and rodent. Consistent with this, our recent study
suggested that transcriptional activation of human -chain
promoter was observed in various types of cells and the
cis-enhancing elements and transcription factors different
from those of mouse identified in this study were involved in the
regulation of human -chain promoter (Y. Akizawa, C. Nishiyama, M.
Hasegawa, K. Maeda, T. Nakahata, K. Okumura, H. Ogawa, and C. Ra,
manuscript in preparation).
The motif (T/A)GATA(A/G) has been well-known as consensus recognition
sequence of GATA-family proteins. However, recently, it was reported
that GATA protein binds a variety of motifs with high affinity
equivalent to that of conventional GATA motif and activates the
transcription activity (20, 21). In this report, we
suggest that GATA-1 protein prepared from PT18 cells binds and
transactivates the -chain promoter via motifs TGATAt (-53/-48,
-46/-51) and TGATtG (-42/-47) as well as the canonical consensus
sequence, AGATAA (-26/-31). A single GATA-1 protein that occupies
either of the overlapping GATA-1 motifs may prevent different GATA-1
proteins from binding the other two GATA-1-motifs by possible steric
hindrance. However, palindromic or overlapping GATA sites were found in
several promoters and were shown to give higher GATA-1-binding affinity
than a promoter with a single GATA site (22). Therefore,
it may be possible to assume that two of the three, at least, GATA-1
motifs are recognized by two GATA-1 proteins. For elucidation of the
mechanism for GATA-1-mediated up-regulation of the promoter via
multiple GATA-1 motifs, detailed analysis including the determination
of three-dimensional structure of whole GATA-1/DNA complex will be
obviously required.
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Acknowledgments |
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Footnotes |
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2 Address correspondence and reprint requests to Dr. Chiharu Nishiyama, Atopy (Allergy) Research Center, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo, 113-8421, Japan. E-mail address: chinishi{at}med.juntendo.ac.jp
Received for publication July 25, 2002. Accepted for publication October 28, 2002.
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References |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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RI): from physiology to pathology. Annu. Rev. Immunol. 17:931.[Medline]
RI) on monocytes of atopic individuals. J. Exp. Med. 179:745.RI as a complex composed of FcRI - and FcRI -chains and can use this receptor for IgE-mediated allergen presentation. J. Immunol. 157:607.[Abstract]
RI). J. Exp. Med. 175:1285. is a molecular amplifier of IgE- and IgG-mediated in vivo responses. Immunity 8:517.[Medline]
-chain gene. J. Immunol. 163:623.RI -chain gene expression by multiple transcription factors. J. Immunol. 168:4546., , and subunits of the high-affinity IgE receptor (FcRI) and intracellular, but not cell surface, subunit protein. J. Allergy Clin. Immunol. 105:309.[Medline]
receptors on murine eosinophils: implications for the functional significance of elevated IgE and eosinophils in parasitic infections. Blood 89:3826.RI on rat eosinophils and macrophages. J. Immunol. 165:1266.This article has been cited by other articles:
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