1999
DOI: 10.1023/a:1008347729176
|View full text |Cite
|
Sign up to set email alerts
|

Untitled

Abstract: Multiprotein bridging factor 1 (MBF1) is a transcriptional coactivator that is thought to bridge between the TATA box-binding protein (TBP) and DNA binding regulatory factors, and is conserved from yeast to human. Human MBF1 (hMBF1) can bind to TBP and to the nuclear receptor Ad4BP, and is suggested to mediate Ad4BP-dependent transcriptional activation. Here we report the resonance assignments and secondary structure of hMBF1 (57-148) that contains both TBP binding and activator binding residues. 15N relaxatio… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

0
5
0

Year Published

2003
2003
2022
2022

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 11 publications
(5 citation statements)
references
References 9 publications
0
5
0
Order By: Relevance
“…Since then, it has been investigated in several other organisms and shown to bridge different transcription factors, containing sequence-specific DNA-binding domains, to TBP, but not to bind directly to DNA (reviewed in de Koning et al, 2009 ), suggesting it functions by recruiting TBP to promoters where transcription factors are found (Ozaki et al, 1999 ). Structural analyses were able to precise that the C-terminal end corresponds to a well-structured helix-turn-helix (HTH) motif (Mishima et al, 1999 ; Ozaki et al, 1999 ).…”
Section: Introductionmentioning
confidence: 99%
“…Since then, it has been investigated in several other organisms and shown to bridge different transcription factors, containing sequence-specific DNA-binding domains, to TBP, but not to bind directly to DNA (reviewed in de Koning et al, 2009 ), suggesting it functions by recruiting TBP to promoters where transcription factors are found (Ozaki et al, 1999 ). Structural analyses were able to precise that the C-terminal end corresponds to a well-structured helix-turn-helix (HTH) motif (Mishima et al, 1999 ; Ozaki et al, 1999 ).…”
Section: Introductionmentioning
confidence: 99%
“…The N- and C-termini sequences are divergent among different organisms, whereas the HTH domain, which contains four α-helices, is conserved 2 . The HTH domain is responsible for the functional activity of MBF1, and differences in the N- and C-termini do not affect the main activities of MBF1 proteins 3 , 4 .…”
Section: Introductionmentioning
confidence: 99%
“…In addition to the MBF1 domain (PF08523), the MBF1 protein includes an HTH XRE-family domain (SM000530), also known as a Cro/C1-type HTH domain (IPR001387), located in the C-terminus, that is annotated as a DNA-binding domain of transcriptional regulators. The HTH XRE domain contains four α-helices, and is responsible for MBF1 function [2527]. In the present study, purified recombinant rPoxMBF1 protein could directly bind to the promoter regions of major cellulase and xylanase genes in vitro, thereby controlling their transcriptional levels in P .…”
Section: Discussionmentioning
confidence: 80%