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PLENARY PAPER
From the Hematology/Oncology Division, Harvard
Institute of Medicine, Harvard Medical School, and the
Hematology/Oncology Division, Children's Hospital and the Dana Farber
Cancer Institute, the Department of Pediatrics, Harvard Medical School,
Howard Hughes Medical Institute, Boston, MA; and the Department
of Immunology and Molecular and Experimental Medicine, The Scripps
Research Institute, La Jolla, CA.
The lineage-specific transcription factors GATA-1 and
PU.1 can physically interact to inhibit each other's function,
but the mechanism of repression of GATA-1 function by PU.1 has not been elucidated. Both the N terminus and the C terminus of PU.1 can physically interact with the C-terminal zinc finger of GATA-1. It
is demonstrated that the PU.1 N terminus, but not the C
terminus, is required for inhibiting GATA-1 function. Induced
overexpression of PU.1 in K562 erythroleukemia cells blocks
hemin-induced erythroid differentiation. In this system, PU.1 does not
affect the expression of GATA-1 messenger RNA, protein, or
nuclear localization. However, GATA-1 DNA binding decreases
dramatically. By means of electrophoretic mobility shift assays with
purified proteins, it is demonstrated that the N-terminal 70 amino
acids of PU.1 can specifically block GATA-1 DNA binding. In addition,
PU.1 had a similar effect in the G1ER cell line, in
which the GATA-1 null erythroid cell line G1E has been transduced with
a GATA-1-estrogen receptor fusion gene, which is directly
dependent on induction of the GATA-1 fusion protein to effect erythroid
maturation. Consistent with in vitro binding assays, overexpression of
PU.1 blocked DNA binding of the GATA-1 fusion protein as well as
GATA-1-mediated erythroid differentiation of these G1ER cells. These
results demonstrate a novel mechanism by which function of a
lineage-specific transcription factor is inhibited by another
lineage-restricted factor through direct protein-protein
interactions. These findings contribute to understanding how
protein-protein interactions participate in hematopoietic
differentiation and leukemogenesis.
(Blood. 2000;96:2641-2648) Transcription factors, acting in a combinatorial
fashion, play a critical role in the differentiation of hematopoietic
lineages.1 As the expression of lineage-specific factors
overlaps in early progenitor cells, choice of lineage may be controlled
in part through protein-protein interactions that lead either to
functional synergy or to inhibition. There are many examples of
protein-protein interactions that result in functional synergy,
including GATA-1 and Friend of GATA-1 (FOG-1) in
erythroid cells,2 PU.1 and PU.1 interaction
partner (Pip) in B cells,3,4 and PU.1 and c-Jun
in myeloid cells.5 The potential for inhibitory
interactions between transcription factors is implied by the
observations that overexpression of GATA-1 (or GATA-2) or PU.1 blocks
myeloid or erythroid differentiation, respectively.6-12
Functional repression could result either from decreased expression of
the target transcription factor or from inhibition of that protein's
function. The latter possibility is supported by the recent finding
that PU.1 and GATA-1 physically interact to inhibit each other's
function.10,11,13
GATA-1 regulates the expression of many erythroid genes, is highly
expressed in erythroid cells, and is required for terminal differentiation of erythroid precursors.14,15 GATA-1
contains 2 zinc fingers. The carboxyl (C) finger is essential for DNA
binding, and the amino-terminal (N) zinc finger stabilizes
binding.16 Mutation of one of the cysteines in the
C-finger of GATA-1 abolishes DNA binding and results in loss of
transactivation function.17 GATA-1 is not appreciably
expressed in myeloid cells. Enforced expression of GATA-1 in the
progenitor line 416B or multipotential avian precursors blocks myeloid
differentiation and induces erythroid, megakaryocytic, and eosinophilic
characteristics.6,8 GATA-1 is expressed in some cases of
myeloid and megakaryocytic transformation of chronic myelogenous
leukemia (CML) into blast crisis but not in lymphoid blast
crisis of CML.18 Taken together, these data suggest that
expression of GATA-1 may inhibit myeloid differentiation and may be
involved in the development of certain types of myeloid leukemia.
The ETS family member PU.1 is a myeloid and B-cell-specific
transcription factor that is highly expressed in Friend-virus-induced erythroleukemia.19 Overexpression of PU.1 in long-term
culture of bone marrow cells is able to stimulate proliferation but
blocks differentiation of proerythroblasts.20 Similarly,
overexpression of PU.1 in mouse erythroleukemia cell lines results in a
block in chemically induced erythroid differentiation21 and
a decrease in the expression of the erythroid marker
The mechanism by which PU.1 blocks erythroid differentiation is
unclear. We and others have reported that PU.1 physically interacts
with GATA-1 and represses GATA-1 function in vitro and in
vivo.10,11,13 We previously demonstrated that a small
region ( Cell culture and development of cell lines expressing PU.1
Northern blot analysis
Western blot analysis Whole-cell lysates were made by lysis of cell pellets with a modified RIPA buffer containing 50 mmol/L Tris-HCl (pH 7.4), 1% NP-40, 0.25% sodium deoxycholate, 150 mmol/L NaCL, 1 mmol/L EGTA, 1 mmol/L phenylmethylsulfonyl fluoride, and proteinase inhibitors. Nuclear protein from K562, K562/PU.1, G1ER, and G1ER/PU.1 cells were isolated as described.33 Then, 60 µg of whole-cell lysate or 30 µg of nuclear protein were fractionated on a 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) gel and transferred to nylon membranes. A 1:1000 dilution of rabbit anti-PU.1 polyclonal antibody (sc-352; Santa Cruz Biotechnology, Santa Cruz, CA) or rat anti-GATA-1 monoclonal antibody (sc-265, Santa Cruz Biotechnology) was used to detect protein expression. The amount of -actin or tubulin in each lane was detected by a mouse antimouse
-actin monoclonal antibody (Sigma, St Louis, MO), or
antitubulin monoclonal antibodies (Santa Cruz Biotechnology, Santa
Cruz, CA) were used as loading controls for gels with whole-cell lysates. The amount of Sp1 protein detected by goat anti-Sp1 polyclonal antibody (sc-59X7, Santa Cruz Biotechnology) was used as a loading control for gels fractionating nuclear proteins. After incubation with
the first antibody, the proteins were detected with an appropriate secondary antibody conjugated with horseradish peroxidase and a
chromogen substrate (ECL; Amersham, Uppsala, Sweden).
Purification of glutathione-S-transferase fusion proteins and electrophoretic mobility shift assays Glutathione-S-transferase (GST) fusion proteins were expressed in BL21 Escherichia coli and purified as described.34 The GST fusion proteins were eluted from the glutathione agarose beads with 20 mmol/L glutathione, 50 mmol/L Tris-HCl (pH 7.5), and 150 mmol/L NaCl for 20 minutes at room temperature, followed by dialysis with 50 mmol/L Tris-Cl and 150 mmol/L NaCl overnight at 4°C. Eluted proteins were then concentrated on Microcon columns (Amicon, Neceolah, WI) according to the manufacturer's procedure. Electrophoretic mobility shift assays (EMSAs) were performed as described.35 The oligonucleotide in GATA-binding assays was GGCAACTGATAAGGATTC and was end-labeled with 32P- -ATP (adenosine triphosphate) and polynucleotide
kinase.17 The oligonucleotide for detecting
octamer binding was AAGAGATTTATGCAAACGGGATGGG.36 The
oligonucleotide for detecting GST-ETS binding was TCGAATA AAATCAGGAACTTG.36
PU.1 retroviral expression vector The construction, packaging, and infection have been previously described.37 Briefly, the complete PU.1 coding region was isolated by polymerase chain reaction and inserted into the retroviral expression vector pBA8b-L1, termed pBA8b-L1.PU.1. It also contains the human placental alkaline phosphatase gene under the control of the cytomegalovirus promoter 3' of the inserted PU.1 cDNA. Production of a stable pBA8b-L1.PU.1 amphotropic line and the generation of infectious supernatant were performed as described.37 To transduce G1ER cells, the wells of a 6-well tissue culture plate were first coated with fibronectin (Sigma), and then virus supernatant was added to allow viral particles to adhere. Cells were then added in the presence of 8 µg/mL polybrene, and the plate was centrifuged at 1000g for 3 hours at room temperature. After centrifugation, the cells were cultured in regular medium for 24 hours. The whole procedure was repeated 3 times.Transient transfection The protocol for transfection of CV-1 cells by the calcium phosphate precipitation method has been described.38 Lipofectamine transfections were performed according to the manufacturer's procedure (Gibco BRL, Rockville, MD). At 4 hours after transfection, cells were placed in 10% fetal bovine serum and incubated for another 40 hours, and firefly luciferase activity was measured as relative light units (RLUs). The RLUs from individual transfections were normalized by measurement of Renilla luciferase activity expressed from a cytomegalovirus-promoter-driven vector in the same samples.39 Individual transfection experiments were performed in triplicate, and the results are reported as mean firefly RLUs/Renilla (± SD).
PU.1 does not affect GATA-1 mRNA, protein expression, or translocation to the nucleus The mechanisms by which PU.1 expression blocks erythropoiesis has not been fully described.10,11,25 In the erythroid cell line MEL, PU.1 overexpression blocks dimethyl sulfoxide induction of erythroid differentiation, and the expression of-globin
decreases.9 It has been previously shown that the
important regulatory elements of the -globin gene have GATA-1
sites.22 These studies suggest that PU.1 inhibition of
GATA-1 function blocks erythropoiesis. To further investigate the
mechanism of PU.1 repression of GATA-1 function, we generated K562 cell
lines stably transfected with the PU.1 cDNA driven by the
zinc-inducible metallothionein promoter. We analyzed 2 clones
(K562/mPU.1 no. 3 and K562/mPU.1 no. 7) in detail. The expression of
exogenous PU.1 mRNA (data not shown) and protein (Figure
1B) was induced with 100 µmol/L
ZnSO4 in 8 hours. Erythroid differentiation was induced in
K562 cells with 2.5 × 10 5 hemin, and the appearance of
erythroid cells monitored with benzidine staining. As shown in Table
1, after hemin induction, but in the
absence of ZnSO4-induced PU.1 expression, we observed 35% to 46% benzidine-positive cells in K562/pC18 (a line with vector alone), K562/mPU.1 no. 3, and K562/mPU.1 no. 7 cells. When the cells
were treated with hemin in the presence of ZnSO4, the
percentage of benzidine-positive cells in K562/mPU.1 no. 3 and
K562/mPU.1 no. 7 decreased dramatically to 6.7% and 8.9%,
respectively. ZnSO4 had no significant effect on the
differentiation of K562 cells transfected with the metallothionein
vector alone (K562/pC18).
We next wished to determine if PU.1 decreased the expression of GATA-1 mRNA or protein in these lines. In Northern blot analysis, overexpression of PU.1 after zinc induction had no effect on the expression of GATA-1 mRNA for up to 72 hours (Figure 1A). Western analysis of whole-cell lysates at different times after ZnSO4 induction demonstrated that the PU.1 protein was induced (Figure 1B, top panel) and translocated into nuclei (Figure 1C, top panel) at 8 hours after ZnSO4 treatment. However, the level of detectable PU.1 protein remains constant in whole-cell lysates but decreases in nuclear extracts for unknown reasons. Similar results were obtained from multiple experiments. This could be due to altered reactivity of PU.1 to the antibody used for detection.40 The expression of GATA-1 protein was not affected in whole-cell lysates (Figure 1B). The level of GATA-1 protein in the nuclei was assessed to discover whether PU.1 blocked GATA-1 translocation from the cytoplasm. As shown in Figure 1C, the level of GATA-1 protein in the nuclei of K562/PU.1 cells remains unchanged before and after ZnSO4 induction. In summary, expression of PU.1 blocks erythroid differentiation without affecting GATA-1 mRNA, protein expression, or nuclear translocation. The N terminus of PU.1, but not the 3/4 domain within the C-terminal ETS domain of PU.1
interact with GATA-1, and that full-length PU.1 inhibits GATA-1
transactivation.11 To assess which domain of PU.1
contributes to the inhibition of GATA-1 function, transient
transfections were performed with a plasmid consisting of multiple GATA
DNA-binding sites in front of a minimal thymidine kinase promoter
(3XGATA-TK) driving luciferase gene expression as a reporter.
As shown in Figure 2, GATA-1 can activate
the reporter gene expression about 4-fold. GATA-1 transactivation was
fully repressed by cotransfection with wild-type PU.1. Deletion of the
PU.1 N-terminal 70 amino acids resulted in a loss in the ability to
inhibit GATA-1 function; a PU.1 polypeptide with a deletion of the
3/4 region repressed GATA-1 function as well as wild-type PU.1.
Similar results were obtained with cotransfections using PU.1 and
GATA-2 expression plasmids. Therefore, the N terminus of PU.1 interacts
with GATA-1 and is required for PU.1 repression of GATA-1 function. In
contrast, our previous studies indicated that GATA-1 inhibits PU.1
function by directly interacting with the PU.1 3/4 region, thus
blocking interaction with the PU.1 coactivator c-Jun.11
PU.1 blocks GATA-1 binding to DNA Overexpression of PU.1 in the MEL erythroid cell line reduced GATA-1 DNA-binding activity in cell extracts,25 but whether this is a direct or an indirect effect was not determined. We have previously shown that PU.1 interacts with the C-finger of GATA-1,11 which serves as the DNA recognition motif for GATA-1. It is possible that PU.1 blocks GATA-1 binding to DNA owing to direct interaction with this GATA-1 C-finger. To test this hypothesis, an EMSA was performed as shown in Figure 3A. Various GST-PU.1 fusion proteins were used to compete with GATA-1 for binding to an oligonucleotide containing a GATA-binding site. As assessed by SDS-PAGE, 0.1 µg and 0.5 µg of each GST-PU.1 were used for the reactions. Increasing the amount of GST-PU.1 full-length protein decreased GATA-1 DNA binding (Figure 3A, lanes 7 and 8). The PU.1 ETS domain alone did not reduce GATA-1 DNA binding (Figure 3A, lanes 10 and 11); however, it still bound to the PU.1-binding-site oligonucleotide as shown in Figure 3A, right panel (lanes 2 and 3), indicating that it is folded properly. The N-terminal 70 amino acids of PU.1 could block GATA-1 binding to DNA as effectively as the full-length PU.1 protein (Figure 3A, lanes 13 and 14). Interestingly, deletion of the N-terminal 100 amino acids and the3/4 region of PU.1 were not only unable
to inhibit GATA-1 DNA binding, but appeared to enhance GATA-1 DNA
binding and induced the formation of slower migrating complexes (Figure
3A, lanes 16-17), perhaps as a result of oligomerization of GATA-1
under these conditions.43 These data suggest that PU.1
blocks GATA-1 binding to DNA by direct interaction with the GATA-1
C-finger. To exclude the possibility that PU.1 represses GATA-1
function through the GATA-1 activation domain, we performed transient
transfections using a fusion protein between GATA-1 N- and C-zinc
fingers (as a DNA-binding domain) and the VP16 transactivation
domain (N + C-VP16) as an activator, and the 3XGATA-TK luciferase as
a reporter. As shown in Figure 3B, the N + C-VP16 protein activated
the GATA-1 reporter nearly 3-fold. Although this activation was modest,
it was consistently observed in multiple experiments. As expected, full-length PU.1 but not the N-terminal 70-amino acid deletion of PU.1
inhibited the fusion protein transactivation function, even though the
protein level of the truncated protein was higher than that of
wild-type PU.1 in the transfected CV-1 cells, as shown in Figure 3B,
right panel. These results demonstrate that inhibition of GATA-1 DNA
binding can block transactivation.
We next investigated whether PU.1 blocks GATA-1 binding to DNA in K562
cells. Nuclear extracts from K562/PU.1 cells at different time points
after induction with hemin alone or hemin plus ZnSO4 were
used for gel shift assays. As shown in Figure
4A, when K562/PU.1 cells were induced
with hemin alone, the expression of GATA-1 protein did not increase,
but GATA-1 DNA-binding activity increased 3.6-fold 48 hours after
induction. When PU.1 expression was induced with ZnS04 at
the same time as hemin, the expression of GATA-1 protein remained the
same at all distinct time points, but the DNA-binding activity of
GATA-1 decreased dramatically (Figure 4B).
PU.1 blocks GATA-1-dependent erythroid cell differentiation by inhibiting GATA-1 DNA binding To further analyze if PU.1 inhibition of GATA-1 DNA binding blocks erythroid cell differentiation in vivo, we used G1ER cells. These cells were derived from GATA-1-deficient embryonic stem cells transfected with a GATA-1-ER fusion protein and differentiate to mature red blood cells in response to exogenous-estradiol.2,44 G1ER cells were transduced with a viral
construct harboring the PU.1 cDNA. We analyzed 2 G1ER/PU.1 lines
derived from separate clones. Mock transduced G1ER cells (G1ER/M) were
used as a control. As shown in Figure 5A
and Table 1, when the G1ER/M cells were treated with -estradiol, the
percentage of benzidine-positive cells increased in 48 hours from below
0.5% to 52%. In contrast, only 5.6 to 6.8% benzidine-positive cells
were observed in G1ER/PU lines (which express high levels of PU.1)
after -estradiol stimulation. To obtain another marker of erythroid
differentiation, we measured the expression of erythroid-specific
major-globin mRNA expression in G1ER/M and G1ER/PU cells after
-estradiol induction (Figure 5C). The expression of major-globin
mRNA increased markedly in G1ER cells but remained at the same low
levels in G1ER/PU cells after -estradiol induction. Therefore,
expression of PU.1 inhibited the ability of GATA-1 to induce erythroid
differentiation of these cells.
To investigate whether PU.1 blocked GATA-1-ER binding to DNA in G1ER
cells, nuclear proteins were isolated from G1ER/M and G1ER/PU cells at
different times after
We and others have recently reported that PU.1 physically
interacts with GATA-1.10,11,13 These physical interactions
result in repression in which PU.1 and GATA-1 inhibit each other's
function. Previously, we demonstrated that GATA-1 interacts with the
GATA-1 contains 2 zinc fingers. The N-terminal zinc finger mediates interaction with the GATA-1 coactivator FOG, which is essential for erythroid development.2 The C-terminal zinc finger not only serves as a DNA-recognition motif,17 but also contributes to self-association43 and protein-protein interactions with the coactivator CBP.45 This functionally important domain interacts with 2 distinct regions of PU.1, a transcription factor that is functionally divergent from GATA-1. PU.1 has been reported to decrease GATA-1 binding to DNA during the induction of apoptosis by overexpression of PU.1 in MEL cells, an erythroid cell line that expresses GATA-1, but the mechanism of how PU.1 inhibited GATA-1 DNA binding was not elucidated.25 GATA-1 inhibits PU.1 function by inhibiting binding of the PU.1 coactivator c-Jun.5 The GATA-1 N-finger, not the C-finger, interacts with the coactivator, FOG.2 Our previous results indicated that both domains of PU.1 interacted with the GATA-1 C-finger, but not the FOG-binding N-finger.11 These results, combined with the studies presented here, suggest that blocking DNA binding rather than inhibition of a coactivator mediates the repression of GATA-1 by PU.1, whereas the opposite is true for the mechanism of inhibition of PU.1 by GATA-1 (Figure 6).11 We hypothesized that the mechanism of PU.1 repression of GATA-1
function was from direct interaction with the C-finger of GATA-1, which
inhibits GATA-1 DNA binding. Our hypothesis was supported by the
results from our EMSA studies, in which a PU.1 polypeptide containing
the first 70 amino acids inhibited GATA-1 DNA binding, and a fragment
containing the C-terminal PU.1 ETS domain had no effect (Figure 3A).
Interestingly, a PU.1 mutant peptide with deletions of both regions of
PU.1 interacting with the GATA-1 C-finger demonstrated increased DNA
binding as well as more slowly migrating complexes (Figure 3A). These
results imply that the interaction of the PU.1 Further evidence supporting the role of the PU.1 N terminus blocking
GATA-1 DNA binding was the ability of full-length PU.1, but not a
mutant that lacked the N terminus but retained the K562 and G1ER cells were used as models to investigate whether PU.1 blocks GATA-1 DNA binding in erythroid cells. PU.1 blocks GATA-1 DNA binding in both cell lines and blocks erythroid differentiation as shown in Figures 4B and 5. It is interesting that PU.1 inhibits GATA-1 DNA binding in K562 cells only when the cells are induced with hemin. PU.1 does not block GATA-1 DNA binding when PU.1 expression is induced in the absence of erythroid differentiation induction in K562/PU.1 cells (data not shown). The same result was reported in MEL cells.25 These data suggest that during erythroid differentiation, GATA-1 protein might undergo modifications, such as phosphorylation or acetylation, that affect the ability of PU.1 to block DNA binding. Both phosphorylation48 and acetylation49 have been reported to increase GATA-1 DNA-binding activity. PU.1 might only inhibit phosphorylated and/or acetylated GATA-1 binding to DNA. In summary, the N terminus of PU.1, and not the What are the consequences of these interactions? These repressive interactions appear to be required not only for induction of differentiation in normal myelopoiesis and erythropoiesis, but also during the process of hematopoietic lineage commitment. Such interactions are consistent with a model in which hematopoietic stem cells express simultaneously low levels of "lineage-specific" transcription factors, such as GATA-1 and PU.1, and lineage commitment is characterized by activation of one transcription factor pathway and inhibition of the other.12,50 This model is consistent with studies demonstrating that overexpression of PU.1 contributes to the development of murine erythroleukemia mediated by the Friend virus,19 and blocks GATA-1-mediated erythroid differentiation. Similarly, overexpression of GATA-1 inhibits myeloid differentiation, and this requires only the C-terminal finger.7,8,13 Of relevance to human disease is the finding that expression of GATA-1 may contribute to18 or exacerbate51 the block in myeloid differentiation found in acute myeloid leukemia. Understanding the mechanisms involved in interactions between factors such as PU.1 and GATA-1 not only will contribute to our understanding of normal hematopoiesis, but also could lead to novel therapeutic strategies.
We thank Claus Nerlov for sharing ideas and results prior to publication, Margaret Baron and Tim Ley for murine globin probes, Mary Singleton for assistance with preparation of the manuscript, and other members of the Tenen laboratory for useful discussions.
Submitted February 11, 2000; accepted June 13, 2000.
Supported by National Institutes of Health (NIH) grants CA41456 (D.G.T.) and DK659381 (B.E.T.) and additional grants from NIH (S.H.O.). S.H.O. is an Investigator of the Howard Hughes Medical Institute.
The publication costs of this article were defrayed in part by page charge payment. Therefore, and solely to indicate this fact, this article is hereby marked "advertisement" in accordance with 18 U.S.C. section 1734.
Reprints: Daniel G. Tenen, Harvard Institute of Medicine, Rm 954, 77 Ave Louis Pasteur, Boston, MA 02115; e-mail: dtenen{at}caregroup.harvard.edu.
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K. E. Elagib, M. Xiao, I. M. Hussaini, L. L. Delehanty, L. A. Palmer, F. K. Racke, M. J. Birrer, G. Shanmugasundaram, M. A. McDevitt, and A. N. Goldfarb Jun Blockade of Erythropoiesis: Role for Repression of GATA-1 by HERP2 Mol. Cell. Biol., September 1, 2004; 24(17): 7779 - 7794. [Abstract] [Full Text] [PDF]
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F. Rosenbauer, K. Wagner, P. Zhang, K.-P. Knobeloch, A. Iwama, and D. G. Tenen pDP4, a novel glycoprotein secreted by mature granulocytes, is regulated by transcription factor PU.1 Blood, June 1, 2004; 103(11): 4294 - 4301. [Abstract] [Full Text] [PDF]
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C. Cerdan, A. Rouleau, and M. Bhatia VEGF-A165 augments erythropoietic development from human embryonic stem cells Blood, April 1, 2004; 103(7): 2504 - 2512. [Abstract] [Full Text] [PDF]
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M. Joo, G. Y. Park, J. G. Wright, T. S. Blackwell, M. L. Atchison, and J. W. Christman Transcriptional Regulation of the Cyclooxygenase-2 Gene in Macrophages by PU.1 J. Biol. Chem., February 20, 2004; 279(8): 6658 - 6665. [Abstract] [Full Text] [PDF]
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M. Gering, Y. Yamada, T. H. Rabbitts, and R. K. Patient Lmo2 and Scl/Tal1 convert non-axial mesoderm into haemangioblasts which differentiate into endothelial cells in the absence of Gata1 Development, December 22, 2003; 130(25): 6187 - 6199. [Abstract] [Full Text] [PDF]
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N. Rekhtman, K. S. Choe, I. Matushansky, S. Murray, T. Stopka, and A. I. Skoultchi PU.1 and pRB Interact and Cooperate To Repress GATA-1 and Block Erythroid Differentiation Mol. Cell. Biol., November 1, 2003; 23(21): 7460 - 7474. [Abstract] [Full Text] [PDF]
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K. S. Choe, F. Radparvar, I. Matushansky, N. Rekhtman, X. Han, and A. I. Skoultchi Reversal of Tumorigenicity and the Block to Differentiation in Erythroleukemia Cells by GATA-1 Cancer Res., October 1, 2003; 63(19): 6363 - 6369. [Abstract] [Full Text] [PDF]
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M. Rylski, J. J. Welch, Y.-Y. Chen, D. L. Letting, J. A. Diehl, L. A. Chodosh, G. A. Blobel, and M. J. Weiss GATA-1-Mediated Proliferation Arrest during Erythroid Maturation Mol. Cell. Biol., July 15, 2003; 23(14): 5031 - 5042. [Abstract] [Full Text] [PDF]
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M. Eisbacher, M. L. Holmes, A. Newton, P. J. Hogg, L. M. Khachigian, M. Crossley, and B. H. Chong Protein-Protein Interaction between Fli-1 and GATA-1 Mediates Synergistic Expression of Megakaryocyte-Specific Genes through Cooperative DNA Binding Mol. Cell. Biol., May 15, 2003; 23(10): 3427 - 3441. [Abstract] [Full Text] [PDF]
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A. F. Gombart, S. H. Kwok, K. L. Anderson, Y. Yamaguchi, B. E. Torbett, and H. P. Koeffler Regulation of neutrophil and eosinophil secondary granule gene expression by transcription factors C/EBPepsilon and PU.1 Blood, April 15, 2003; 101(8): 3265 - 3273. [Abstract] [Full Text] [PDF]
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J. Cammenga, J. C. Mulloy, F. J. Berguido, D. MacGrogan, A. Viale, and S. D. Nimer Induction of C/EBPalpha activity alters gene expression and differentiation of human CD34+ cells Blood, March 15, 2003; 101(6): 2206 - 2214. [Abstract] [Full Text] [PDF]
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J. Starck, N. Cohet, C. Gonnet, S. Sarrazin, Z. Doubeikovskaia, A. Doubeikovski, A. Verger, M. Duterque-Coquillaud, and F. Morle Functional Cross-Antagonism between Transcription Factors FLI-1 and EKLF Mol. Cell. Biol., February 15, 2003; 23(4): 1390 - 1402. [Abstract] [Full Text] [PDF]
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J. Du, M. J. Stankiewicz, Y. Liu, Q. Xi, J. E. Schmitz, J. A. Lekstrom-Himes, and S. J. Ackerman Novel Combinatorial Interactions of GATA-1, PU.1, and C/EBPepsilon Isoforms Regulate Transcription of the Gene Encoding Eosinophil Granule Major Basic Protein J. Biol. Chem., November 1, 2002; 277(45): 43481 - 43494. [Abstract] [Full Text] [PDF]
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R. Kapur, S. Chandra, R. Cooper, J. McCarthy, and D. A. Williams Role of p38 and ERK MAP kinase in proliferation of erythroid progenitors in response to stimulation by soluble and membrane isoforms of stem cell factor Blood, July 30, 2002; 100(4): 1287 - 1293. [Abstract] [Full Text] [PDF]
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B. U. Mueller, T. Pabst, M. Osato, N. Asou, L. M. Johansen, M. D. Minden, G. Behre, W. Hiddemann, Y. Ito, and D. G. Tenen Heterozygous PU.1 mutations are associated with acute myeloid leukemia Blood, July 18, 2002; 100(3): 998 - 1007. [Abstract] [Full Text] [PDF]
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W. Hong, A. Y. Kim, S. Ky, C. Rakowski, S.-B. Seo, D. Chakravarti, M. Atchison, and G. A. Blobel Inhibition of CBP-Mediated Protein Acetylation by the Ets Family Oncoprotein PU.1 Mol. Cell. Biol., June 1, 2002; 22(11): 3729 - 3743. [Abstract] [Full Text] [PDF]
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K. Kumano, S. Chiba, K. Shimizu, T. Yamagata, N. Hosoya, T. Saito, T. Takahashi, Y. Hamada, and H. Hirai Notch1 inhibits differentiation of hematopoietic cells by sustaining GATA-2 expression Blood, December 1, 2001; 98(12): 3283 - 3289. [Abstract] [Full Text] [PDF]
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Y. Ozawa, M. Towatari, S. Tsuzuki, F. Hayakawa, T. Maeda, Y. Miyata, M. Tanimoto, and H. Saito Histone deacetylase 3 associates with and represses the transcription factor GATA-2 Blood, October 1, 2001; 98(7): 2116 - 2123. [Abstract] [Full Text] [PDF]
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Abstract
Introduction
-dCTP
(deoxycytidine triphosphate) by random primed labeling and
hybridization were performed as described.
N70 is the N-terminal 70-amino
acid PU.1 deletion mutant in pcDNA3; 
