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J Biol Chem, Vol. 273, Issue 43, 27757-27760, October 23, 1998
From the Whitehead Institute for Biomedical Research, Cambridge,
Massachusetts 02142 and Department of Biology, Massachusetts Institute
of Technology, Cambridge, Massachusetts 02139
The RNA polymerase II holoenzyme is the form of
eukaryotic RNA polymerase II that is recruited to the promoters of
protein-coding genes in living cells. The exact composition of the
holoenzyme is not entirely established, due in part to technical
difficulties associated with purifying intact megadalton size
multiprotein complexes. Nonetheless, yeast and human holoenzyme
preparations have been described that consist of near stoichiometric
levels of most components known to be generally involved in initiation other than TATA-binding protein
(TBP)1 and its associated
factors. We review here the functions of five major components of yeast
RNA polymerase II holoenzymes: core RNA polymerase II, the general
transcription factors (GTFs), the core Srb-mediator complex, the Srb10
cyclin-dependent kinase (CDK) complex, and the Swi-Snf
complex (Table I).
The holoenzyme concept stems from the discovery that Srb proteins are
critical for regulated transcription of protein coding genes and the
observation that these proteins are tightly associated with a portion
of core RNA polymerase II in yeast cells (1). The genes encoding the
yeast Srb proteins were discovered through a genetic screen designed to
identify components of the transcription apparatus that are involved in
the response to transcriptional regulators (2, 3). Attempts to purify
these proteins led to the isolation of a large complex containing core
RNA polymerase II, a subset of the general transcription factors, and a
variety of regulatory proteins (1). This holoenzyme complex had the capacity to initiate transcription and respond to activators when supplemented with additional purified general transcription factors in vitro. A subcomplex dissociated from the holoenzyme,
which contains the Srb and additional proteins, reconstituted the
response to activators in a defined in vitro transcription
system (4). The response to activators is especially significant as
in vitro systems reconstituted with yeast GTFs and
polymerase alone are not activator-responsive (5, 6). Two of the yeast
Srb proteins were found to be required for transcription of most
protein-coding genes, and because they are found tightly associated
with the holoenzyme, it seems likely that the Srb-containing holoenzyme is the form of RNA polymerase II that is recruited to most promoters in vivo (7).
RNA polymerase II holoenzymes have been purified from many eukaryotic
organisms (1, 4, 8-16). The subunit composition of these different
preparations differs somewhat, and these differences involve the
presence or absence of two types of components: GTFs and regulatory
factors. Some protocols lead to the purification of RNA polymerase II
holoenzymes containing all of the GTFs (8, 9, 14), whereas other
protocols generate holoenzymes in which only a single GTF (TFIIF)
remains associated (4). Some yeast holoenzyme preparations contain
stoichiometric levels of Swi-Snf (17), whereas others lack any
detectable Swi-Snf protein (18). In the present discussion, we will
make the simplifying assumption that holoenzymes in living cells
resemble the more complex preparations. Thus, the holoenzyme we discuss
here is composed of core RNA polymerase II, all the GTFs other than TBP
(and its associated proteins), the core Srb-mediator complex, the Srb10
cyclin-dependent kinase complex, and the Swi-Snf complex
(Table I).
Eukaryotic core RNA polymerase II (Pol II) was first purified by
using transcription assays with promoterless templates (19, 20). The
purified enzyme typically has 10-12 subunits and is incapable of
specific promoter recognition. Yeast RNA polymerase II consists of 12 subunits, RPB1-RPB12, which range in size from approximately 6 to 200 kDa. A very similar 12-subunit enzyme can be purified from human cells,
and numerous subunit-subunit interactions within the polymerase have
been delineated (21). An interesting feature of the enzyme is the
highly conserved domain at the C terminus of the largest subunit (CTD).
This domain contains multiple repeats of the consensus sequence YSPTSPS
and, as discussed below, is a substrate for several kinases that have
roles in regulation of gene expression.
There is considerable evidence that the eukaryotic enzymes are highly
conserved. Core Pol II molecules purified from a wide range of
eukaryotes have conserved subunit structure and sequence. Moreover,
many yeast Pol II subunit genes can be replaced with their mammalian
counterparts in living cells without deleterious effects on cell
function (22-26). This level of functional conservation is remarkable
considering the thousands of protein coding genes that must be
expressed appropriately for normal cellular function and viability.
General transcription factors were purified for their
ability to facilitate specific promoter recognition by core RNA
polymerase II. Five such factors were found to be essential for this
activity on most promoters used in vitro: TFIID, TFIIB,
TFIIF, TFIIH, and TFIIE. As with core RNA polymerase, the GTFs are
highly conserved among eukaryotes. The precise roles of the GTFs have
been reviewed in detail elsewhere (27) and will not be discussed
here.
Based on the genetic and biochemical evidence to date, we favor the
model that transcription activation at many promoters involves
recruitment of the transcription initiation apparatus in two steps. In
this model, recruitment of two complexes is required for activation: a
TBP-containing complex (reviewed in Ref. 28) and a holoenzyme
containing the remaining GTFs. Although recruitment of either complex
could be sufficient to assemble the other, activators may target
members from both complexes and/or multiple components within a single
complex. This combination of multiple activator-target interactions
would result in transcription. This model does not exclude the
possibility that transcription initiation at some promoters involves
recruitment of components in many steps, and initiation at other
promoters can involve recruitment of the entire apparatus in a single
step. Indeed, given the large number of promoters present in living
cells and the diverse mechanisms known to regulate gene expression, it
seems likely that the entire spectrum of possibilities is realized.
Transcription reactions reconstituted in vitro with
highly purified RNA polymerase II and GTFs are not responsive to
activators. The yeast mediator is a multiprotein complex that was
purified for its ability to mediate activation (4). A less complex
"core" Srb-mediator complex has recently been purified (29). This
core complex consists of 16 polypeptides: Srb2, -4, -5, -6, and -7, Med1, -2, -4, -6, -7, and -8, Gal11, Sin4, Rgr1, Rox3, and Pgd1. These
polypeptides can be separated into several functional groups and are
described in more detail below.
The SRB2, -4, -5, and
-6 genes were identified genetically as dominant, gain of
function, suppressors of yeast RNA polymerase II large subunit CTD
truncation mutants (2, 8, 30). CTD truncation does not appear to reduce
the stability of core RNA polymerase II (31) but does reduce the
ability of the holoenzyme to respond to activators (32-34). It appears
that the SRB gain-of-function mutations compensate for CTD
truncations by affecting the ability of activators to interact with the
holoenzyme (35) and possibly by increasing its stability.
Recombinant Srb2, Srb4, Srb5, and Srb6 can form a stable complex
in vitro (35). Within this complex, Srb2 is associated with
Srb5, and Srb4 is associated with Srb6. An interaction between Srb2 and
Srb4 is responsible for bringing the four proteins together in a single
complex. Srb4 and Srb6 are essential for the transcription of
most, if not all, protein-coding genes (7). Srb2 and Srb5 increase
stable preinitiation complex formation in nuclear extracts but are not
essential for all yeast gene expression (8).
Recent genetic and biochemical studies show that Srb4 is a target
of the yeast activator Gal4 (35). Affinity chromatography, photocross-linking, and surface plasmon resonance experiments all
demonstrated that the Gal4 activator can interact directly with Srb4.
The Gal4 activation domain was found to bind to two essential segments
of Srb4. The physiological relevance of this interaction was confirmed
by isolating gain-of-function mutations in the Gal4-binding domain of
Srb4, which restore activation in vivo by a Gal4 derivative
bearing a mutant activation domain.
SRB7, an essential gene, was identified through a
recessive mutation that restores the viability of yeast CTD truncation
mutants (36). The human SRB7 gene has been cloned and is
functional in yeast when present as a human-yeast chimera (10).
Antibodies against human Srb7 have been used to purify and characterize
mammalian holoenzymes (10, 13, 15, 16). The lack of a conditional mutation in Srb7 or an in vitro system in which Srb-mediator
activity can be reconstituted with purified recombinant proteins has
prevented more detailed analysis of its function.
The Med proteins are the set of polypeptides that are found
in the yeast core mediator complex but which were not previously identified through genetic analysis (Table I) (29, 37). Recent evidence
reveals that the Med proteins are associated with the Srb2, -4, -5, and
-6 complex via an interaction between Med6 and Srb4 (38).
The mediator complex was purified for its ability to reconstitute
activated transcription in an in vitro system with highly purified factors (4); confirmation that the Med proteins contribute to
activated transcription in vivo has come from experiments
employing a conditional mutation in MED6 (39). Strains
harboring a Med6 temperature-sensitive allele are defective for
activation of certain genes in vivo. Holoenzymes prepared
from this strain show mild defects in basal transcription and more
striking defects in activated transcription. Interestingly, these
defects can be rescued by addition of recombinant Med6 protein, and the
activation defect manifests itself only prior to initiation. That is,
after preinitiation complex (PIC) formation, Med6 has no apparent
function.
The members of this group of proteins were identified in a variety
of yeast genetic screens as a result of their influence on repression
of certain genes (40). Mutations in these proteins can cause elevated
expression of genes whose promoters lack upstream-activating sequence
elements (41-46). In this context, they appear to act as repressors,
and they may act to prevent initiation at promoters unless the proper
activation signals are present. Further supporting this idea, loss of
function mutations in Gal11 and Sin4 relieve repression of
GAL genes in the absence of the inducer (42). Sin4 and Rgr1
mutations allow transcription of the HO gene in the absence
of the activator Swi5 (47-49).
Mutations in these proteins can also cause a reduction in activation
for certain genes in vivo (41, 44, 50-52). For example, GAL gene expression in Gal11 mutants can be
activated to just 30% of wild type levels (53). Most of our knowledge
of the functions of Gal11, Sin4, Rgr1, Rox3, and Pgd1 comes from
genetic studies, so it is not clear whether the primary roles of these
proteins involve both positive and negative functions or if their roles in activation are indirect. It seems likely, however, that the primary
roles of these proteins are in negative regulation. RNA polymerase II
holoenzymes lacking these components do not exhibit activation defects
in vitro (54). In cells with deficiencies in these proteins,
the extent of derepression of some genes can be 10-fold or greater
whereas the degree to which activation is reduced is not as
substantial. The increased expression of certain genes because of loss
of repression could cause a reduction in normal activated levels of
expression at highly inducible genes simply because there is
insufficient transcription initiation apparatus to accommodate the
demands of the latter set of genes in the cell.
Analysis of deletion and truncation mutants suggests that Gal11, Sin4,
Rgr1, and Pgd1 form a subcomplex whose interaction with other
components of the mediator is anchored by Rgr1 (54). This biochemical
analysis nicely explains the similarity of the mutant phenotypes.
Srb8, -9, -10, and -11 were identified as recessive suppressors of
CTD truncation mutations (36, 55). These loss of function mutations act
in a manner opposite to the core mediator Srbs (Srb2, -4, -5, -6, and
-7), indicating that they play a negative role in transcription. The
genes encoding Srb8, -9, -10, and -11 were also identified as Ssn5, -2, -3, and -8 in a screen developed to identify suppressors of a loss of
function in the SNF1 gene, and these genes are essential for
complete repression of the glucose-repressed, galactose metabolism
genes (GAL ) (56, 57). Loss of function mutations in this
subcomplex cause derepression of a wide variety of genes (58).
Additionally, Srb10 and -11 function is required for full
Tup1-Ssn6-mediated repression (56, 59).
Srb10 and -11 form a cyclin-dependent kinase-cyclin pair
that phosphorylates serine 5 of the consensus heptapeptide repeat of
the large subunit of RNA polymerase II C-terminal domain (60). Interestingly, this kinase-cyclin pair has the same substrate specificity as the Kin28-Ccl1 kinase-cyclin pair found in the GTF
TFIIH. Kin28 has a positive role in transcription, that of producing a
phosphorylated form of the enzyme which is associated with active
elongation. In contrast, the Srb10 kinase has a negative role in
transcription. Srb10 is uniquely capable of phosphorylating the CTD in
purified holoenzymes prior to template binding, and this
phosphorylation inhibits subsequent transcription by the holoenzyme.
Srb10 does not appear to inhibit transcription after formation of a
stable PIC. Thus, the transcription initiation apparatus can be
regulated positively or negatively via modification of the CTD,
depending on the timing of the phosphorylation event. Srb10 and -11 fires before competent PIC formation, thereby repressing transcription,
and Kin28-Ccl1 fires after PIC formation, creating an
elongation-competent form of polymerase (60).
Srb8 and -9, although not essential for Srb10 and -11 kinase activity
in vitro, are required for their stable association with the
holoenzyme; holoenzyme preparations from Srb8 deletion strains lack
Srb10 and -11.2 It should
prove interesting to identify the control mechanisms for the Srb10
CDK.
Components of the Swi-Snf complex were first identified in two
genetic screens: the loss of ability to switch mating types (Swi) and
the loss of ability to utilize sucrose as a carbon source (Snf). The
11-subunit Swi-Snf complex has been purified (61-63) and exhibits an
ATP-dependent chromatin-destabilizing activity (62). The
Swi-Snf complex is believed to antagonize chromatin-based repression of
transcription in vivo (64, 65).
The Swi-Snf complex has an intrinsic, nonspecific DNA binding activity
(66), posing the quandary of how the complex can be effectively
targeted to specific promoter regions when needed. This problem is
underscored by recent enzymological studies that show that the purified
Swi-Snf enzyme requires over 4 min to remodel one nucleosome on a
nucleosome array (67). At this rate, the complex would require over
35 h to randomly remodel the nucleosomes present in the nucleus
(67). Clearly, this must be a targeted event. The finding that Swi-Snf
is an accessory subcomplex of the holoenzyme (17) provides an
attractive model to explain how Swi-Snf is directed to chromosomal
regions that require local remodeling of chromatin structure for
appropriate gene expression.
The transcription apparatus is recruited to promoters under the
control of DNA-binding gene-specific regulators, and these can have
positive or negative regulatory functions (68, 69). It seems likely
that certain holoenzyme components provide specific interaction
surfaces for activators and others for repressors. For example, the
transcriptional activator Gal4 contacts Srb4, and we speculate that a
promoter-specific factor contacts Srb10 to effect negative regulation
at those promoters.
We presume that the complex machinery in the eukaryotic Pol II
holoenzyme exists in part to permit a broad range of regulatory capabilities. The ability to recruit this intricate machinery to
promoters provides the opportunity to regulate the same apparatus in
different ways at different promoters, yet allows for coregulation of
sets of genes and the flexibility necessary to respond to changing environments. Genome-wide expression monitoring with mutations in
various holoenzyme subunits, together with further study of the
interactions between transcriptional regulators and holoenzyme components, could reveal how this is accomplished.
Many of the yeast holoenzyme components discussed here have known
homologues in higher eukaryotic cells. As mentioned previously, core
RNA polymerase II and the GTFs are highly conserved among eukaryotes.
Human Swi-Snf complexes have been purified that share structural and
functional attributes with their yeast counterpart (70). Components of
the yeast core Srb-mediator complex and the Srb10
cyclin-dependent kinase complex are also found in mammalian cells. These include human Srb7 (hSrb7), human Med6, and human Srb10
and -11 (CDK8-cyclin C)(9-11, 13-16). Thus, the gene regulatory mechanisms at work in the yeast Saccharomyces cerevisiae are
likely conserved in all eukaryotes. The isolation and characterization of mammalian Srb-mediator complexes should lead to a more sophisticated understanding of these regulatory mechanisms and might help uncover the
mechanisms behind some cell-type specific differences in gene expression.
*
This minireview will be reprinted
in the 1998 Minireview Compendium, which
will be available in December, 1998.
The abbreviations used are:
TBP, TATA-binding
protein; GTF, general transcription factor; CDK, cyclin-dependent kinase; Pol, polymerase; CTD, C-terminal
domain; PIC, preinitiation complex.
2
S.-M. Liao and R. A. Young, unpublished
data.
MINIREVIEW
RNA Polymerase II Holoenzymes and Subcomplexes*
INTRODUCTION
Top
Introduction
References
RNA polymerase II holoenzyme components in S. cerevisiae
Core RNA Polymerase II
The General Transcription Factors
The Core Srb-Mediator Complex
Srb2, -4, -5, and -6 Subcomplex
Srb7
Med Proteins
Gal11, Sin4, Rgr1, Rox3, and Pgd1/Hrs1/Med3
Srb10 CDK and Associated Polypeptides
Swi-Snf
Holoenzyme Subcomplexes and Gene Regulation
Holoenzymes and Subcomplexes in Higher Eukaryotes
FOOTNOTES
To whom correspondence should be addressed: Whitehead Inst. for
Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142. Tel.:
617-258-5218; Fax: 617-258-0376; E-mail: young{at}wi.mit.edu.
REFERENCES
Top
Introduction
References
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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Q. Tan, X. Li, P. P. Sadhale, T. Miyao, and N. A. Woychik Multiple Mechanisms of Suppression Circumvent Transcription Defects in an RNA Polymerase Mutant Mol. Cell. Biol., November 1, 2000; 20(21): 8124 - 8133. [Abstract] [Full Text]
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S. M. Carty, A. C. Goldstrohm, C. Suñé, M. A. Garcia-Blanco, and A. L. Greenleaf Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II PNAS, July 19, 2000; (2000) 160266597. [Abstract] [Full Text]
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D. R. Dorris and K. Struhl Artificial Recruitment of TFIID, but Not RNA Polymerase II Holoenzyme, Activates Transcription in Mammalian Cells Mol. Cell. Biol., June 15, 2000; 20(12): 4350 - 4358. [Abstract] [Full Text]
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T. Kotani, K.-i. Banno, M. Ikura, A. G. Hinnebusch, Y. Nakatani, M. Kawaichi, and T. Kokubo A role of transcriptional activators as antirepressors for the autoinhibitory activity of TATA box binding of transcription factor IID PNAS, June 13, 2000; (2000) 120074297. [Abstract] [Full Text]
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E. Castaño, P. Gross, Z. Wang, R. G. Roeder, and T. Oelgeschläger The C-terminal domain-phosphorylated IIO form of RNA polymerase II is associated with the transcription repressor NC2 (Dr1/DRAP1) and is required for transcription activation in human nuclear extracts PNAS, June 13, 2000; (2000) 140202297. [Abstract] [Full Text]
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N. Chiba, Z. Suldan, L. P. Freedman, and J. D. Parvin Binding of Liganded Vitamin D Receptor to the Vitamin D Receptor Interacting Protein Coactivator Complex Induces Interaction with RNA Polymerase II Holoenzyme J. Biol. Chem., April 6, 2000; 275(15): 10719 - 10722. [Abstract] [Full Text] [PDF]
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Y. Tsukihashi, T. Miyake, M. Kawaichi, and T. Kokubo Impaired Core Promoter Recognition Caused by Novel Yeast TAF145 Mutations Can Be Restored by Creating a Canonical TATA Element within the Promoter Region of the TUB2 Gene Mol. Cell. Biol., April 1, 2000; 20(7): 2385 - 2399. [Abstract] [Full Text]
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S. Kim, K. Cabane, M. Hampsey, and D. Reinberg Genetic Analysis of the Ydr1-Bur6 Repressor Complex Reveals an Intricate Balance among Transcriptional Regulatory Proteins in Yeast Mol. Cell. Biol., April 1, 2000; 20(7): 2455 - 2465. [Abstract] [Full Text]
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S. Hahn and S. Roberts The zinc ribbon domains of the general transcription factors TFIIB and Brf: conserved functional surfaces but different roles in transcription initiation Genes & Dev., March 15, 2000; 14(6): 719 - 730. [Abstract] [Full Text]
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Q. Tan, K. L. Linask, R. H. Ebright, and N. A. Woychik Activation mutants in yeast RNA polymerase II subunit RPB3 provide evidence for a structurally conserved surface required for activation in eukaryotes and bacteria Genes & Dev., February 1, 2000; 14(3): 339 - 348. [Abstract] [Full Text]
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N. K. Conrad, S. M. Wilson, E. J. Steinmetz, M. Patturajan, D. A. Brow, M. S. Swanson, and J. L. Corden A Yeast Heterogeneous Nuclear Ribonucleoprotein Complex Associated With RNA Polymerase II Genetics, February 1, 2000; 154(2): 557 - 571. [Abstract] [Full Text]
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 S. Pan, E. Czarnecka-Verner, and W. B. Gurley Role of the TATA Binding Protein-Transcription Factor IIB Interaction in Supporting Basal and Activated Transcription in Plant Cells PLANT CELL, January 1, 2000; 12(1): 125 - 136. [Abstract] [Full Text] [PDF]
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J. G. Gall, M. Bellini, Z.'a. Wu, and C. Murphy Assembly of the Nuclear Transcription and Processing Machinery: Cajal Bodies (Coiled Bodies) and Transcriptosomes Mol. Biol. Cell, December 1, 1999; 10(12): 4385 - 4402. [Abstract] [Full Text]
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J. Yie, K. Senger, and D. Thanos Mechanism by which the IFN-beta enhanceosome activates transcription PNAS, November 9, 1999; 96(23): 13108 - 13113. [Abstract] [Full Text] [PDF]
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D. P. Morris, H. P. Phatnani, and A. L. Greenleaf Phospho-Carboxyl-Terminal Domain Binding and the Role of a Prolyl Isomerase in Pre-mRNA 3'-End Formation J. Biol. Chem., October 29, 1999; 274(44): 31583 - 31587. [Abstract] [Full Text] [PDF]
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M. Patturajan, N. K. Conrad, D. B. Bregman, and J. L. Corden Yeast Carboxyl-terminal Domain Kinase I Positively and Negatively Regulates RNA Polymerase II Carboxyl-terminal Domain Phosphorylation J. Biol. Chem., September 24, 1999; 274(39): 27823 - 27828. [Abstract] [Full Text] [PDF]
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M. Tudor, P. J. Murray, C. Onufryk, R. Jaenisch, and R. A. Young Ubiquitous expression and embryonic requirement for RNA polymerase II coactivator subunit Srb7 in mice Genes & Dev., September 15, 1999; 13(18): 2365 - 2368. [Abstract] [Full Text]
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S. Y. Wu, M. C. Thomas, S. Y. Hou, V. Likhite, and C. M. Chiang Isolation of Mouse TFIID and Functional Characterization of TBP and TFIID in Mediating Estrogen Receptor and Chromatin Transcription J. Biol. Chem., August 13, 1999; 274(33): 23480 - 23490. [Abstract] [Full Text] [PDF]
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 T. J. Darcy, W. Hausner, D. E. Awery, A. M. Edwards, M. Thomm, and J. N. Reeve Methanobacterium thermoautotrophicum RNA Polymerase and Transcription In Vitro J. Bacteriol., July 15, 1999; 181(14): 4424 - 4429. [Abstract] [Full Text]
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C. Sune and M. A. Garcia-Blanco Transcriptional Cofactor CA150 Regulates RNA Polymerase II Elongation in a TATA-Box-Dependent Manner Mol. Cell. Biol., July 1, 1999; 19(7): 4719 - 4728. [Abstract] [Full Text] [PDF]
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 P. R. Cook The Organization of Replication and Transcription Science, June 11, 1999; 284(5421): 1790 - 1795. [Abstract] [Full Text]
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N. A. Hawkes and S. G. E. Roberts The Role of Human TFIIB in Transcription Start Site Selection in Vitro and in Vivo J. Biol. Chem., May 14, 1999; 274(20): 14337 - 14343. [Abstract] [Full Text] [PDF]
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M. Mannervik, Y. Nibu, H. Zhang, and M. Levine Transcriptional Coregulators in Development Science, April 23, 1999; 284(5414): 606 - 609. [Abstract] [Full Text]
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J. D. Fondell, M. Guermah, S. Malik, and R. G. Roeder Thyroid hormone receptor-associated proteins and general positive cofactors mediate thyroid hormone receptor function in the absence of the TATA box-binding protein-associated factors of TFIID PNAS, March 2, 1999; 96(5): 1959 - 1964. [Abstract] [Full Text] [PDF]
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D. Balciunas, C. Galman, H. Ronne, and S. Bjorklund The Med1 subunit of the yeast mediator complex is involved in both transcriptional activation and repression PNAS, January 19, 1999; 96(2): 376 - 381. [Abstract] [Full Text] [PDF]
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F. C. P. Holstege and R. A. Young Transcriptional regulation: Contending with complexity PNAS, January 5, 1999; 96(1): 2 - 4. [Full Text] [PDF]
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 Y. LUO and R.G. ROEDER B-cell-specific Coactivator OCA-B: Biochemical Aspects, Role in B-Cell Development and Beyond Cold Spring Harb Symp Quant Biol, January 1, 1999; 64(0): 119 - 132. [Abstract] [PDF]
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J. A. Ranish, N. Yudkovsky, and S. Hahn Intermediates in formation and activity of the RNA polymerase II preinitiation complex: holoenzyme recruitment and a postrecruitment role for the TATA box and TFIIB Genes & Dev., January 1, 1999; 13(1): 49 - 63. [Abstract] [Full Text]
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J. I. Adamkewicz, C. G. F. Mueller, K. E. Hansen, W. A. Prud'homme, and J. Thorner Purification and Enzymic Properties of Mot1 ATPase, a Regulator of Basal Transcription in the Yeast Saccharomyces cerevisiae J. Biol. Chem., July 7, 2000; 275(28): 21158 - 21168. [Abstract] [Full Text] [PDF]
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J. Saez-Vasquez and C. S. Pikaard RNA Polymerase I Holoenzyme-Promoter Interactions J. Biol. Chem., November 17, 2000; 275(47): 37173 - 37180. [Abstract] [Full Text] [PDF]
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Y. Liu, J. A. Ranish, R. Aebersold, and S. Hahn Yeast Nuclear Extract Contains Two Major Forms of RNA Polymerase II Mediator Complexes J. Biol. Chem., March 2, 2001; 276(10): 7169 - 7175. [Abstract] [Full Text] [PDF]
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J. I. Adamkewicz, K. E. Hansen, W. A. Prud'homme, J. L. Davis, and J. Thorner High Affinity Interaction of Yeast Transcriptional Regulator, Mot1, with TATA Box-binding Protein (TBP) J. Biol. Chem., April 6, 2001; 276(15): 11883 - 11894. [Abstract] [Full Text] [PDF]
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R. L. Woodard, K.-j. Lee, J. Huang, and W. S. Dynan Distinct Roles for Ku Protein in Transcriptional Reinitiation and DNA Repair J. Biol. Chem., April 27, 2001; 276(18): 15423 - 15433. [Abstract] [Full Text] [PDF]
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S.-Y. Wu and C.-M. Chiang TATA-binding Protein-associated Factors Enhance the Recruitment of RNA Polymerase II by Transcriptional Activators J. Biol. Chem., August 31, 2001; 276(36): 34235 - 34243. [Abstract] [Full Text] [PDF]
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Y.-S. Dai and B. E. Markham p300 Functions as a Coactivator of Transcription Factor GATA-4 J. Biol. Chem., September 28, 2001; 276(40): 37178 - 37185. [Abstract] [Full Text] [PDF]
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T. Kotani, K.-i. Banno, M. Ikura, A. G. Hinnebusch, Y. Nakatani, M. Kawaichi, and T. Kokubo A role of transcriptional activators as antirepressors for the autoinhibitory activity of TATA box binding of transcription factor IID PNAS, June 20, 2000; 97(13): 7178 - 7183. [Abstract] [Full Text] [PDF]
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E. Castano, P. Gross, Z. Wang, R. G. Roeder, and T. Oelgeschlager The C-terminal domain-phosphorylated IIO form of RNA polymerase II is associated with the transcription repressor NC2 (Dr1/DRAP1) and is required for transcription activation in human nuclear extracts PNAS, June 20, 2000; 97(13): 7184 - 7189. [Abstract] [Full Text] [PDF]
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S. M. Carty, A. C. Goldstrohm, C. Sune, M. A. Garcia-Blanco, and A. L. Greenleaf Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II PNAS, August 1, 2000; 97(16): 9015 - 9020. [Abstract] [Full Text] [PDF]
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E. A. Felinski and P. G. Quinn The coactivator dTAFII110/hTAFII135 is sufficient to recruit a polymerase complex and activate basal transcription mediated by CREB PNAS, November 6, 2001; 98(23): 13078 - 13083. [Abstract] [Full Text] [PDF]
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