1
National Institutes of Health, National Institute of Child Health and Human
Development, Cell Biology and Metabolism Branch, Building 18T, Room 101,
Bethesda, MD 20892, USA
2
Zentrum fur Molekulare Biologie der Universtät
Heidelberg (ZMBH), Im Neunheimer Feld 282, Heidelberg 69120, Germany
*
Author for correspondence (e-mail:
f.sauer{at}mail.zmbh.uni-heidelberg.de
)
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SUMMARY |
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Key words: TAFII250, TFIID, Histone acetyltransferase, Kinase, Ubiquitination, Chromatin, Transcription
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Introduction |
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TAFII250 is one of 10-12 TATA-binding protein (TBP)-associated
factors (TAFIIs) that are complexed with TBP in TFIID (Albright and
Tjian, 2000; Aoyagi and
Wassarman, 2000
). Binding of
TFIID to a core promoter surrounding the transcription start site of a gene
nucleates assembly of the PIC, which contains RNA polymerase II (RNA pol II)
and GTFs TFIIA, TFIIB, TFIIE, TFIIF and TFIIH (Orphanides et al.,
1996
; Hampsey,
1998
). The nucleating function
of TFIID is thought to comprise several distinct activities: (1)
activator-dependent recognition of core promoter DNA sequence elements; (2)
the generation of a chromatin environment that is favorable to PIC assembly
and transcription initiation; and (3) structural modification of GTFs to
facilitate PIC assembly and transcription initiation. TAFII250
contributes to each of these TFIID activities. Recent excitement about
TAFII250 stems from its involvement in regulating the association
of TFIID with the core promoter initiator element and its intrinsic enzymatic
activities that post-translationally modify GTFs and histones. Here, we review
recent studies of TAFII250 and suggest a model for how
TAFII250 activities contribute to gene-specific transcriptional
activation in the context of chromatin.
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TAFII250 is a broadly acting regulator of transcription |
---|
The essential nature of TAFII250 can be attributed to its broad
requirement during RNA-pol-II-dependent transcription. In Drosophila,
TAFII250 is expressed in all nuclei and binds to a large number of
euchromatic sites on polytene chromosomes (Rabenstein et al.,
1999; Wassarman et al.,
2000
). In yeast, genome-wide
microarray analysis indicates that expression of 14-27% of
RNA-pol-II-transcibed genes is downregulated >twofold upon
TAFII145 inactivation (Lee et al.,
2000
). Finally, in
ts13 hamster cells that harbor a temperature-sensitive allele of
TAFII250, similar analysis indicates that the transcription of 18%
of genes transcribed by RNA pol II is affected >twofold at the
non-permissive temperature (O'Brien and Tjian,
2000
). As anticipated, given
the phenotype of TAFII250 mutants, many genes showing
TAFII250-dependent expression encode proteins that are involved in
cell cycle regulation and growth control (Wang and Tjian,
1994
; Walker et al.,
1997
; Lee et al.,
2000
; O'Brien and Tjian,
2000
).
TAFII250 could play a more extensive role in transcription than
these studies predict, since temperature-sensitive mutations might not
inactivate all TAFII250 functions (Dikstein et al.,
1996; Dunphy et al.,
2000
; Lee et al.,
2000
; Tsukihashi et al.,
2000
). There is considerable
disagreement among researchers about the extent to which TAFIIs in
general are required for RNA pol II transcription (Moqtaderi et al.,
1996
; Walker et al.,
1996
; Komarnitsky et al.,
1999
; Lee et al.,
2000
). Part of this
controversy results from the fact that a subset of TAFIIs are
components of other transcriptional regulatory complexes, which makes it
difficult to resolve the contribution of a TAFII to TFIID activity
(Bell and Tora, 1999
). However,
even in the case of TAFII250, which appears to be unique to TFIID,
this is a difficult question to address, since there are factors that can
bypass a requirement for some TAFII250 functions.
A growing list of factors can rescue cell cycle arrest of, or block
apoptosis of, ts13 or tsBN462 hamster cells, which contain
an identical glycine-to-aspartate missense mutation in TAFII250
(Hayashida et al., 1994). This
list includes viral proteins (simian virus 40 (SV40) large T antigen (Damania
and Alwine, 1996
), hepatitis B
virus pX (Haviv et al., 1998
),
human cytomegalovirus (HCMV) immediate-early (IE) proteins IEP86 and IEP72
(Lukak and Alwine, 1999), and human papilloma virus (HPV) 16 E7 (Sekiguchi et
al., 1999
)) and cellular
proteins (E2F-1 (Sekiguchi et al.,
1999
), CIITA (Raval et al.,
2001
) and D-type cyclins
(Sekiguchi et al., 1999
)). Two
distinct mechanisms are involved: overexpression of viral proteins or CTIIA
rescues cells by activating TAFII250-dependent promoters in the
absence of functional TAFII250, whereas overexpression of E2F-1 and
D-type cyclins rescues cells by providing the downstream targets of
TAFII250 activity. SV40 large T antigen, HCMV IE and CIITA proteins
bind to TAFIIs in vitro and in vivo, and mutations that affect
TAFII interactions are unable to rescue the ts13 or
tsBN462 transcriptional defects (Damania and Alwine,
1996
; Mahanta et al.,
1997
; Lukak and Alwine, 1999).
Furthermore, rescue by CTIIA depends on its acetyltransferase activity (Raval
et al., 2001
). Since
TAFII250 acetyltransferase activity is impaired in tsBN462
cells (discussed below), this suggests that CIITA substitutes for
TAFII250 by performing two of its functions: association with TFIID
and acetylation of proteins. Thus, other viral and cellular proteins that
rescue ts13 or tsBN462 cell defects and associate with TFIID
might also be acetyltransferases or affiliate with an acetyltransferase.
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TAFII250 is not the only scaffold for TFIID in vivo |
---|
|
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TAFII250 function is regulated by activators |
---|
Distinct lines of evidence point to a mechanism by which activators bind to
TAFII250 to tether TFIID to particular promoters
(Fig. 2). (1) The region of
ICP4 required for transcriptional activation is also required for
TAFII250 association (Carrozza and DeLuca,
1996). (2) Gene-specific
promoter occupancy of TAFII145 in yeast is elevated in response to
an activation signal and is reduced after removal of enhancer sites (Kuras et
al., 2000
; Li et al.,
2000
). (3) Enhancers can
confer TAFII250 dependence on promoters that are normally
TAFII250 independent (Wang et al.,
1997
). Once recruited to a
promoter, TAFII250 could participate in PIC assembly by binding to
the RAP74 subunit (also designated TFIIF
) of TFIIF, as suggested by the
finding that TAFII250 mutants that fail to interact with RAP74 are
unable to rescue the ts13 cell cycle defect (Ruppert and Tjian,
1995
). Tethering of TFIID to
particular genes through activator-TAFII250 binding is advantageous
because TFIID is limiting in cells (Walker et al.,
1996
). The importance of
TAFII250 interactions with both activators and GTFs argues that
TAFII250 functions as a classically defined coactivator that
bridges activators to PIC assembly.
|
There is also ample support for a mechanism in which activators modify
TAFII250 activities to enhance formation or stability of the PIC on
promoter DNA (Fig. 2).
Competitive interplay between activators and TAFII250 could control
binding of TFIID to core promoters. The N-terminus of TAFII250
binds to the DNA-binding surface of TBP and inhibits TBP-DNA interactions
(Kotani et al., 1998).
However, acidic activators, JUN and TFIIA compete with TAFII250 for
binding to TBP, thus altering the DNA-binding properties of TFIID (Kokubo et
al., 1998
; Ozer et al.,
1998
; Kotani et al.,
2000
; Lively et al.,
2001
). Moreover, some
repressors inhibit TAFII250 enzymatic activities (discussed below)
that may promote PIC assembly by modifying the structure of GTFs and
chromatin. Binding of HIV Tat, an activator and repressor of viral gene
transcription, to TAFII250 inhibits TAFII250 HAT
activity (Weissman et al.,
1998
). Similarly, binding of
RB to TAFII250 inhibits TAFII250 N-terminal kinase
activity (Siegert and Robbins,
1999
; Solow et al.,
2001
). In contrast, E1A and
cyclin D1 suppress the TAFII250-kinase-inhibitory effect of RB
(Siegert et al., 2000
). Thus,
regulation of TAFII250 activities by interactions with activators
and GTFs is integral to the process of transcriptional activation.
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TAFII250 binds to core promoter initiator sequences |
---|
Analysis of core promoters of genes whose expression is affected by
TAFII250 mutations does not clarify the role of the TATA element in
specifying TAFII250 dependence. Some TAFII250-dependent
promoters contain a nonconsensus TATA element, whereas others contain a
consensus TATA element (Moqtaderi et al.,
1996; Shen and Green,
1997
). Insertion of a
canonical TATA element into a TATA-less promoter can bypass a dependence on
TAFII145, but mutation of a weak TATA element to the consensus
sequence does not change the requirement for TAFII145 (Shen and
Green, 1997
; Tsukihashi et
al., 2000
). Thus, there
appears to be a sophisticated code composed of contributions from TATA and Inr
core promoter elements that specifies TAFII250 dependence.
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TAFII250 post-translationally modifies histones and GTFs |
---|
TAFII250 is a bipartite protein kinase
TAFII250 contains two independent serine/threonine protein
kinase domains: one at the N-terminus (NTK) and the other at the C-terminus
(CTK; Dikstein et al., 1996;
O'Brien and Tjian, 1998
;
Fig. 1). Kinase activity has
been demonstrated in vitro for the Drosophila, human and yeast
proteins. Yeast is unusual in that the kinase domains reside in two separate
proteins. TAFII145 and Bromodomain factor 1 (Bdf1) contain the NTK
and CTK, respectively (Mantangkasonbut et al., 2000).
The TAFII250 NTK and CTK domains autophosphorylate, and the NTK
domain transphosphorylates RAP74 and the large subunit of TFIIA (TFIIA-L) in
vitro (Dikstein et al., 1996;
Solow et al., 2001
). RAP74 and
TFIIA are reasonable candidates as substrates for TAFII250 kinase
activity in vivo: endogenous RAP74 is hyperphosphorylated; dephosphorylation
of RAP74 reduces its ability to support transcription elongation in vitro; and
phosphorylation of TFIIA stimulates TFIIA-TBP-TATA-element complex formation
in vitro (Kitajima et al.,
1994
; Solow et al.,
2001
;
Fig. 2). Autophosphorylation by
TAFII250 might also play a regulatory role in transcription, as has
been shown for TFIIF (Rossignol et al.,
1999
). Despite the lack of
definitive substrates, it is clear that kinase activity is required in vivo,
because a recombinant TAFII250 protein that lacks the NTK domain
cannot rescue ts13 phenotypes (O'Brien and Tjian,
1998
; O'Brien and Tjian,
2000
). Moreover, deletion of
the CTK in Drosophila results in lethality (V. Jo, J. G. Shanklin, E.
M. Schlag and D.A.W., unpublished).
TAFII250 is a histone acetyltransferase and binds to
acetylated histones
Mizzen et al. using an in-gel activity assay, showed that
TAFII250 has HAT activity (Mizzen et al.,
1996). The HAT domain maps to
the central, most conserved portion of metazoan TAFII250 and the
C-terminal portion of yeast TAFII145
(Fig. 1). Many studies have
established a correlation between acetylation of highly conserved lysine
residues in the N-terminal tails of histones and transcriptional activation
(Strahl and Allis, 2000
). One
model to explain how histone acetylation affects gene expression proposes that
the extent of chromatin condensation is directly related to the level of
histone acetylation. Accordingly, hyperacetylation reduces the affinity of
histone tails for DNA, resulting in less compact chromatin and increased
accessibility of transcription factors to DNA.
In vitro, Drosophila TAFII250 acetylates free histones
and nucleosomal histones weakly, relative to yeast HAT1 and human P/CAF
(Mizzen et al., 1996;
Wassarman et al., 2000
). Lys14
of histone H3 is the preferred site of acetylation, although other lysine
residues in H3 and H4 are good substrates for TAFII250 (Mizzen et
al., 1996
).
TAFII250 also acetylates TFIIEß and TFIIF in vitro (Imhof et
al., 1997
) Evidence for the in
vivo importance of TAFII250 HAT activity comes from ts13
and tsBN462 cells. The ability of mutant TAFII250 to
acetylate histones in vitro is temperature sensitive, suggesting that the
enzymatic activity is compromised in ts13 cells at the nonpermissive
temperature and that cell cycle and transcriptional defects observed at the
nonpermissive temperature result from reduced HAT activity (Dunphy et al.,
2000
).
Although histones and GTFs are substrates for TAFII250
acetyltransferase activity in vitro, it is unclear whether they are
transcriptionally relevant substrates. Two lines of evidence indicate that
histones might not be relevant substrates in vitro: (1) transcriptional
activation is temperature sensitive from non-chromatin templates in
ts13 cells extracts; and (2) inhibition of TAFII250
acetyltransferase activity by HIV Tat represses transcription from
non-chromatin templates in HeLa cell extracts (Wang and Tjian,
1994; Weissman et al.,
1998
). Thus, the
TAFII250 acetyltransferase activity is necessary in vitro even in
the absence of histones. Furthermore, TFIIEß and TFIIF might not be
relevant substrates in vitro, because no proteins are acetylated in
reconstituted transcription reactions containing purified GTFs (including
TFIID, TFIIEß and TFIIF), RNA pol II and an activator (Galasinski et al.,
2000
). However, it remains an
open question whether GTFs and histones are acetylated by TAFII250
in vivo. Acetylation of histones by TAFII250 in vivo might produce
a localized change in chromatin structure to enhance accessibility and binding
of TFIID and other PIC components (Fig.
2).
In addition to acetylating proteins, TAFII250 binds to multiply
acetylated histones through two tandem bromodomains located in the C-terminal
region of the protein (Jacobson et al.,
2000;
Fig. 1). The bromodomain is an
120-residue motif present in a variety of proteins that associate with
chromatin (Jeanmougin et al.,
1997
). The TAFII250
double bromodomain (DBD) binds most tightly to histone H4 acetylated at lys5
and lys12 (Jacobson et al.,
2000
). This is consistent with
the crystal structure of the DBD, which shows that the binding pockets for
acetyllysine span a distance equivalent to seven residues. Therefore, the
TAFII250 bromodomains may target TFIID to chromatin-packaged
promoters (Fig. 2).
TAFII250 is a ubiquitin-activating/conjugating enzyme
Most recently, TAFII250 has been demonstrated to mediate
monoubiquitination of histone H1, a linker histone that binds to DNA between
adjacent nucleosomes (Crane-Robinson,
1999; Pham and Sauer,
2000
). In vitro,
monoubiquitination requires the sequential activity of ubiquitin-activating
(E1) and ubiquitin-conjugating (E2) enzymes (Ciechanover et al.,
2000
). TAFII250
contains both of these activities: it becomes covalently linked, via a
thioester bond, to ubiquitin in an ATP-dependent manner (E1 activity), and it
transfers activated ubiquitin to histone H1 via an isopeptide bond (E2
activity; Pham and Sauer,
2000
). The E1 and E2
activities of Drosophila and human TAFII250 reside in the
central region of the protein (Fig.
1). Most intriguingly, this region is absent from yeast
TAFII145 and Bdf1, and, whereas a histone-H1-like protein (HHO1)
has been reported in yeast, it is not known whether it is functionally
homologous to metazoan H1 proteins (Ushinsky et al.,
1997
).
Mutations in Drosophila TAFII250 that impair histone H1
ubiquitination activity in vitro and in vivo were isolated in a genetic screen
for genes that modulate the ability of the Ras GTPase to specify cell fates
(Karim et al., 1996; Wassarman
et al., 2000
). Gene targets
for TAFII250 in Ras signaling pathways have not been identified,
but TAFII250 mutations do affect transcription in the
Drosophila embryo, reducing the expression of Dorsal and Caudal
target genes (Pham and Sauer,
2000
; A.-D. Pham and F.S.,
unpublished). It is unclear how monoubiquitination of histone H1 by
TAFII250 mediates transcription. One attractive model, based on the
ability of H1 to facilitate the folding of nucleosomal arrays into
higher-order structures, is that ubiquitination changes the chromatin-binding
properties of H1 and thereby destabilizes both local and higher-order
chromatin structures and alters core histone-DNA interactions (Crane-Robinson,
1999
; Mizzen and Allis,
2000
;
Fig. 2). Indeed, binding of
histone H1 to chromatin is highly dynamic in living cells, and modulation of
H1 binding activity is thought to be an important step in regulating access of
the transcriptional machinery to DNA (Lever et al.,
2000
; Misteli et al.,
2000
).
While TAFII250 does not require an E3 ubiquitin-ligase to
monoubiquitinate histone H1 in vitro, it is possible that it utilizes one to
ubiquitinate other proteins in vivo. An excellent candidate for this enzyme is
the MDM2 ubiquitin ligase, whose binding to TAFII250 correlates
with transcriptional activation (Honda et al.,
1997; Leviellard and Wasylyk,
1997). In vivo, MDM2 may target the E1 and E2 activities of
TAFII250 to proteins such as p53 (Buschmann et al.,
2000
).
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Conclusions and perspectives: a model for the role of TAFII250 during transcriptional activation |
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In summary, this simplistic model describes how individual tools contained
within a TAFII250 `toolbox' contribute to the conversion of
activation signals received by TFIID into the enzymatic synthesis of messenger
RNA. We anticipate that the model will undergo numerous refinements as in vivo
substrates for TAFII250 activities are defined, the molecular
consequences of these modifications are determined, and high-resolution
structures of TAFII250, TFIID and the PIC are solved (Andel et al.,
1999).
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ACKNOWLEDGMENTS |
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