Identification of the core domain and the secondary structure of the transcriptional coactivator MBF1

Ozaki, Jun; Takemaru, Ken Ichi; Mishima, Masaki; Ueda, Hitoshi; Hirose, Susumu; Kabe, Yoshio; Handa, Hiroshi; Shirakawa, Masahiro

doi:10.1046/j.1365-2443.1999.00267.x

Cited by 19 publications

(13 citation statements)

References 39 publications

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“…The region conserved in Drosophila MBF1 includes both of these functional domains (Fig. 1A) (Ozaki et al, 1999). Expression of Drosophila mbf1 cDNA partially rescued the yeast mbf1 mutant phenotype upon amino acid starvation (Fig.…”

Section: Characterization Of Drosophila Mbf1mentioning

confidence: 92%

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DrosophilaMBF1 is a co-activator for Tracheae Defective and contributes to the formation of tracheal and nervous systems

et al. 2003

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INTRODUCTIONTranscriptional regulation plays a major role in the expression of the genomic information during complex biological processes such as differentiation and development. The effect of binding of transcription factors to cis-acting DNA sequences must somehow be transmitted to RNA polymerase to ensure the initiation and maintenance of active transcription. A class of proteins called co-activators serve this role by recruiting the general transcription machinery and by modifying the chromatin structure (Näär et al., 2001;Roeder, 1991). Although sequence-specific DNA-binding transcription factors provide most of the spatial and temporal specificity of expression, the expressional and functional properties of coactivators are also likely to participate in determining the kinetics and efficiency of transcription.Two classes of transcriptional co-activators have been described to date. The first class comprises proteins that possess or recruit enzymatic activities to modify chromatin proteins, e.g. by acetylation of histones. Resulting alteration in the chromatin structure causes a switch in the 'state' of chromatin between transcriptionally inactive and active. Coactivators of the second class act more directly to recruit the general transcription machinery to a promoter where a transcription factor is bound. Among the latter class are TATA element-binding protein (TBP)-associated factors (TAFs) that are subunits of TFIID, and others that serve as adaptors to mediate the contact between transcription factors and the basal transcriptional complex. Although the importance of the first type co-activators for gene expression has been demonstrated (Akimaru et al., 1997;Brownell et al., 1996;Chakravarti et al., 1996;Grant et al., 1997;Kamei et al., 1996;Ogryzko et al., 1996;Waltzer and Bienz, 1999), little is known about how the second class co-activators function in vivo, or how the two types interact to achieve elaborate regulation of gene expression.Multiprotein bridging factor 1 (MBF1) was first identified from the silkmoth as a co-factor necessary for transcriptional activation in vitro by a nuclear receptor FTZ-F1 (Li et al., 1994;Takemaru et al., 1997). The ability of MBF1 to bind both FTZ-F1 and TBP suggested a mechanistic model in which MBF1 recruits TBP to a promoter carrying the FTZ-F1-binding site by interconnecting FTZ-F1 and TBP. The MBF1 sequence is highly conserved across species from yeast to human (Takemaru et al., 1997). In the yeast Saccharomyces cerevisiae, MBF1 functions as a co-activator of a bZIP transcription factor GCN4, by bridging between GCN4 and TBP in response to amino acid starvation (Takemaru et al., 1998).To analyze the biological role of MBF1 in a multicellular organism, we characterized its ortholog in Drosophila. The Drosophila mbf1 gene partially rescued the phenotype of a S. cerevisiae mbf1 -mutant, establishing that both the structure

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Section: Characterization Of Drosophila Mbf1mentioning

confidence: 92%

“…1A). MBF1 consists of two structural domains: a well-structured C-terminal half that binds the general transcription factor TBP; and a flexible Nterminal half that participates in binding to various activators (Ozaki et al, 1999). The region conserved in Drosophila MBF1 includes both of these functional domains (Fig.…”

Section: Characterization Of Drosophila Mbf1mentioning

confidence: 99%

DrosophilaMBF1 is a co-activator for Tracheae Defective and contributes to the formation of tracheal and nervous systems

et al. 2003

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“…NMR studies of hMBF1 and BmMBF1 indeed revealed a well structured C-terminal HTH core. It contains four α-helices and a conserved tail, proposed to be responsible for maintaining domain stability [16,17]. Binding of MBF1 to DNA-binding regulators occurs via the central region, residues 35-113 in B. mori, that also contains the HTH core [6].…”

Section: Sequence and Structurementioning

confidence: 99%

“…In eukaryotes, it has low conservation, and NMR studies indicate a relatively high flexibility [16,17]. In archaea, it contains a conserved zinc-ribbon motif, predicted on the basis of its two pairs of cysteine residues.…”

Section: Sequence and Structurementioning

confidence: 99%

“…It does not affect histone modification, but rather acts as a bridging factor between a DNA-binding protein and the entire TFIID complex [TBP and TAFs (TBPassociated factors)] [3,5,6,12,17,19,20,[24][25][26][27]. DNA-binding proteins that have been reported to interact with MBF1 belong to two protein families: the family of steroid/nuclear hormone receptors, and the family of the bZIPs (basic leucine zippers).…”

Section: Transcription Activationmentioning

confidence: 99%

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Role of multiprotein bridging factor 1 in archaea: bridging the domains?

Koning

Blombach

et al. 2009

Biochemical Society Transactions

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MBF1 (multiprotein bridging factor 1) is a highly conserved protein in archaea and eukaryotes. It was originally identified as a mediator of the eukaryotic transcription regulator BmFTZ-F1 (Bombyx mori regulator of fushi tarazu). MBF1 was demonstrated to enhance transcription by forming a bridge between distinct regulatory DNA-binding proteins and the TATA-box-binding protein. MBF1 consists of two parts: a C-terminal part that contains a highly conserved helix-turn-helix, and an N-terminal part that shows a clear divergence: in eukaryotes, it is a weakly conserved flexible domain, whereas, in archaea, it is a conserved zinc-ribbon domain. Although its function in archaea remains elusive, its function as a transcriptional co-activator has been deduced from thorough studies of several eukaryotic proteins, often indicating a role in stress response. In addition, MBF1 was found to influence translation fidelity in yeast. Genome context analysis of mbf1 in archaea revealed conserved clustering in the crenarchaeal branch together with genes generally involved in gene expression. It points to a role of MBF1 in transcription and/or translation. Experimental data are required to allow comparison of the archaeal MBF1 with its eukaryotic counterpart.

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Joint laxity and the relationship between muscle strength and functional ability in patients with osteoarthritis of the knee

Esch¹,

Steultjens²,

Knol³

et al. 2006

Arthritis & Rheumatism

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Objective. To establish the impact of knee joint laxity on the relationship between muscle strength and functional ability in osteoarthritis (OA) of the knee. Methods. A cross-sectional study of 86 patients with OA of the knee was conducted. Tests were performed to determine varus-valgus laxity, muscle strength, and functional ability. Laxity was assessed using a device that measures the angular deviation of the knee in the frontal plane. Muscle strength was measured using a computer-driven isokinetic dynamometer. Functional ability was assessed by observation (100-meter walking test) and self report (Western Ontario and McMaster Universities Osteoarthritis Index [WOMAC]). Regression analyses were performed to assess the impact of joint laxity on the relationship between muscle strength and functional ability. Results. In regression analyses, the interaction between muscle strength and joint laxity contributed to the variance in both walking time (P ‫؍‬ 0.002) and WOMAC score (P ‫؍‬ 0.080). The slope of the regression lines indicated that the relationship between muscle strength and functional ability (walking time, WOMAC) was stronger in patients with high knee joint laxity. Conclusion. Patients with knee OA and high knee joint laxity show a stronger relationship between muscle strength and functional ability than patients with OA and low knee joint laxity. Patients with OA, high knee joint laxity, and low muscle strength are most at risk of being disabled.

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Identification of the core domain and the secondary structure of the transcriptional coactivator MBF1

Cited by 19 publications

References 39 publications

DrosophilaMBF1 is a co-activator for Tracheae Defective and contributes to the formation of tracheal and nervous systems

DrosophilaMBF1 is a co-activator for Tracheae Defective and contributes to the formation of tracheal and nervous systems

Role of multiprotein bridging factor 1 in archaea: bridging the domains?

Joint laxity and the relationship between muscle strength and functional ability in patients with osteoarthritis of the knee

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