Premium
TBP‐interacting protein TIP120A is a new global transcription activator with bipartite functional domains
Author(s) -
Kayukawa Kentaro,
Kitajima Yoko,
Tamura Takaaki
Publication year - 2001
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1046/j.1365-2443.2001.00407.x
Subject(s) - biology , tata box binding protein , general transcription factor , rna polymerase ii , transcription (linguistics) , transcription factor , taf2 , transcription factor ii b , dna binding protein , transcription factor ii a , eukaryotic transcription , microbiology and biotechnology , transcription factor ii d , genetics , rna polymerase , promoter , rna , enhancer , gene , gene expression , linguistics , philosophy
Background We previously identified a TBP (TATA‐binding protein)‐interacting protein 120A (TIP120A) from rat liver nuclear extracts. TIP120A is thought to be a unique global transcription factor that can interact with TBP and can stimulate all classes of eukaryotic transcription. Results We produced various truncation proteins of TIP120A to delineate its functional domains. TIP120A binds to TBP in the acidic amino acid‐rich N‐terminal region and in the leucine‐rich C‐terminal region. These regions exhibited an ability to stimulate basal transcription in vitro . In addition, these two regions overlap with domains that facilitate nonspecific DNA‐binding of RNA polymerase II. The sequences of these two regions are significantly conserved among TIP120A homologues of eukaryotes. Conclusions TIP120A is a bipartite transcription factor, and both N‐terminal and C‐terminal regions exhibit TBP‐binding activity and stimulate the basal transcription ability.