PMID- 10567521
OWN - NLM
STAT- MEDLINE
DCOM- 20000106
LR  - 20190508
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 12
DP  - 1999 Dec
TI  - TATA-Binding protein-interacting protein 120, TIP120, stimulates three classes of
      eukaryotic transcription via a unique mechanism.
PG  - 7951-60
AB  - We previously identified a novel TATA-binding protein (TBP)-interacting protein
      (TIP120) from the rat liver. Here, in an RNA polymerase II (RNAP
      II)-reconstituted transcription system, we demonstrate that recombinant TIP120
      activates the basal level of transcription from various kinds of promoters
      regardless of the template DNA topology and the presence of TFIIE/TFIIH and
      TBP-associated factors. Deletion analysis demonstrated that a 412-residue
      N-terminal domain, which includes an acidic region and the TBP-binding domain, is
      required for TIP120 function. Kinetic studies suggest that TIP120 functions
      during preinitiation complex (PIC) formation at the step of RNAP II/TFIIF
      recruitment to the promoter but not after the completion of PIC formation.
      Electrophoretic mobility shift assays showed that TIP120 enhanced PIC formation, 
      and TIP120 also stimulated the nonspecific transcription and DNA-binding activity
      of RNAP II. These lines of evidence suggest that TIP120 is able to activate basal
      transcription by overcoming a kinetic impediment to RNAP II/TFIIF integration
      into the TBP (TFIID)-TFIIB-DNA-complex. Interestingly, TIP120 also stimulates
      RNAP I- and III-driven transcription and binds to RPB5, one of the common
      subunits of the eukaryotic RNA polymerases, in vitro. Furthermore, in mouse
      cells, ectopically expressed TIP120 enhances transcription from all three classes
      (I, II, and III) of promoters. We propose that TIP120 globally regulates
      transcription through interaction with basal transcription mechanisms common to
      all three transcription systems.
FAU - Makino, Y
AU  - Makino Y
AD  - Department of Biology, Faculty of Science, Chiba University, and CREST Japan
      Science and Technology Corporation, Inage-ku, Chiba 263-8522, Japan.
FAU - Yogosawa, S
AU  - Yogosawa S
FAU - Kayukawa, K
AU  - Kayukawa K
FAU - Coin, F
AU  - Coin F
FAU - Egly, J M
AU  - Egly JM
FAU - Wang, Z x
AU  - Wang Zx
FAU - Roeder, R G
AU  - Roeder RG
FAU - Yamamoto, K
AU  - Yamamoto K
FAU - Muramatsu, M
AU  - Muramatsu M
FAU - Tamura, T a
AU  - Tamura Ta
LA  - eng
SI  - GENBANK/D87671
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (CAND1 protein, human)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (TATA-Box Binding Protein)
RN  - 0 (Tip120A protein, rat)
RN  - 0 (Transcription Factors)
RN  - EC 2.7.7.- (RNA Polymerase II)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - Cell Line
MH  - DNA-Binding Proteins/metabolism
MH  - Eukaryotic Cells
MH  - *Gene Expression Regulation
MH  - HeLa Cells
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Promoter Regions, Genetic
MH  - RNA Polymerase II/metabolism
MH  - Rabbits
MH  - Rats
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - TATA-Box Binding Protein
MH  - Transcription Factors/genetics/*metabolism
MH  - *Transcription, Genetic
MH  - Transcriptional Activation
MH  - Tumor Cells, Cultured
PMC - PMC84880
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - 10.1128/mcb.19.12.7951 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 Dec;19(12):7951-60. doi: 10.1128/mcb.19.12.7951.