The activation domain of the MotA transcription factor from bacteriophage T4

Finnin, Michael S.; Cicero, Marco P.; Davies, Christopher; Porter, Stephanie; White, Stephen W.; Kreuzer, Kenneth N.

doi:10.1093/emboj/16.8.1992

Cited by 41 publications

(35 citation statements)

References 48 publications

(69 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We speculated that positioning an interaction between MotA and the C-terminal region of 70 would be reasonable, given that residues within region 4.2 of 70 normally interact with the Ϫ35 sequences of the DNA and that the MotA binding site is centered at Ϫ30 (52). The work here demonstrates that the NTD of MotA, which contains residues needed for activation (14,18), can interact with the C-terminal region of 70 . In addition, we have shown that a C-terminal peptide of MotA starting at amino acid 102 can bind DNA with a binding constant similar to that of the full-length protein.…”

Section: Vol 184 2002mentioning

confidence: 72%

“…Residues within the NTD of MotA are required for MotA activation (14,18). Induced synthesis of a cI-MotA NTD fusion, which contained MotA amino acids 1 to 97, in cells containing the ␣-70 chimera resulted in a significant increase in ␤-galactosidase activity (Fig.…”

mentioning

confidence: 94%

“…Nuclear magnetic resonance and crystallographic studies indicate that the 211 amino acids of MotA are organized into an N-terminal domain (NTD) and a C-terminal domain (CTD) separated by a small flexible linker (15,33,34). Mutations within the NTD of MotA eliminate transcriptional activation and the formation of the MotA-70 complex (14,18), suggesting that the NTD is the activation domain of MotA.…”

mentioning

confidence: 99%

See 2 more Smart Citations

The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ⁷⁰Subunit ofEscherichia coliRNA Polymerase

et al. 2002

View full text Add to dashboard Cite

Transcription from bacteriophage T4 middle promoters uses Escherichia coli RNA polymerase together with the T4 transcriptional activator MotA and the T4 coactivator AsiA. AsiA binds tightly within the C-terminal portion of the 70 subunit of RNA polymerase, while MotA binds to the 9-bp MotA box motif, which is centered at ؊30, and also interacts with 70 A programmed cascade of transcriptional events is initiated when bacteriophage T4 infects its host Escherichia coli (reviewed in reference 57). T4 early genes are transcribed immediately after infection by using the existing host RNA polymerase holoenzyme comprising the core (␣ 2 ␤␤Ј) and the 70 subunit. Early T4 promoters do not require T4-encoded transcription factors, since they contain excellent matches to the ideal 70 sequences in their Ϫ10 and Ϫ35 regions (61; reviewed in reference 60). In contrast, transcription from T4 middle promoters uses two T4 early gene products, the transcriptional activator MotA and the coactivator AsiA (23,39,43,44; reviewed in reference 57). Late promoter utilization requires the replacement of 70 by the T4 sigma factor, gp55, as well as other phage-encoded activators and coactivators (reviewed in reference 62).The MotA protein binds as a monomer (6, 33) to a 9-bp element (MotA box) centered at position Ϫ30 of middle promoter DNA (3,19,23). In addition, MotA forms a complex with 70 (18). Nuclear magnetic resonance and crystallographic studies indicate that the 211 amino acids of MotA are organized into an N-terminal domain (NTD) and a C-terminal domain (CTD) separated by a small flexible linker (15,33,34 (44,55,56). Binding sites for AsiA have been mapped within C-terminal amino acids (regions 4.1 and 4.2) of 70 (8,49,50,53,59). Residues within region 4.2 normally contact the Ϫ35 element of host promoter DNA (5,9,17,29,54). In the absence of MotA, AsiA binding to 70 inhibits transcription by polymerase from promoters that require recognition of the Ϫ35 canonical sequences (8,45,51), suggesting that the presence of AsiA inhibits the 70 region 4.2-DNA interaction. In this paper we show that the interaction of a MotA Nterminal peptide (amino acids 1 to 97) with 70 , like the interaction of AsiA with 70 , involves the C-terminal region of 70 . In addition, deletions of the amino acids within the far-Cterminal region of 70 (amino acids 604 to 613) impair the ability of RNA polymerase to perform MotA-dependent activation in vitro. We also show that a MotA C-terminal peptide, beginning at amino acid 102, binds DNA with an apparent dissociation constant like that of wild-type MotA. Our results support a model for MotA-dependent activation in which the interaction between the DNA-bound MotA and the C-terminal region of 70 helps to substitute functionally for an interaction between 70 and a promoter Ϫ35 element. MATERIALS AND METHODSStrains. E. coli KS1 (12) contains a chromosomal lacZ reporter gene under the control of a derivative of the lac promoter P lac that carries a lambda operator (O R 2) centered at position Ϫ62 in place of the ...

show abstract

Section: Vol 184 2002mentioning

confidence: 72%

mentioning

confidence: 94%

mentioning

confidence: 99%

See 1 more Smart Citation

The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ⁷⁰Subunit ofEscherichia coliRNA Polymerase

et al. 2002

View full text Add to dashboard Cite

show abstract

“…The rpd1-2 and rpd1-1 mutations occur in the first and second domains, respectively, suggesting that these domains are important for the function of RPD1. It is notable that these domains might be structurally related to the winged helix proteins, which are involved in various regulatory functions through DNA binding, RNA binding, or protein-protein interaction (Clark et al, 1993;Ramakrishnan et al, 1993;Fogh et al, 1994;Finnin et al, 1997;Groft et al, 1998;Schwartz et al, 1999;Zheng et al, 1999;Gajiwala and Burley, 2000;Okuda et al, 2000;Kamada et al, 2001;Schwartz et al, 2001;Wilce et al, 2001;Selmer and Su, 2002;Zheng et al, 2002;Alfano et al, 2004;Dong et al, 2004;Wei et al, 2004). Studies focusing on this unique structure should provide insight into the molecular function shared by the RPD1 family proteins.…”

Section: Rpd1 Belongs To a Novel Protein Family Specific To The Plantmentioning

confidence: 99%

A Novel Plant-Specific Family Gene, ROOT PRIMORDIUM DEFECTIVE 1, Is Required for the Maintenance of Active Cell Proliferation

Konishi

Sugiyama

2006

Plant Physiology

View full text Add to dashboard Cite

Hypocotyl segments of Arabidopsis (Arabidopsis thaliana) produce adventitious roots in response to exogenously supplied auxin. root primordium defective 1 (rpd1) is a temperature-sensitive mutant isolated on the basis of impairment in this phenomenon. This study describes further phenotypic analysis of the rpd1 mutant and isolation of the RPD1 gene. When adventitious root formation was induced from the rpd1 explants at the restrictive temperature, cell proliferation leading to root promordia formation was initiated at the same time as in wild-type explants. However, development of the root primordia was arrested thereafter in the mutant. Temperature-shift experiments indicated that RPD1 exerts its function before any visible sign of root primordium formation. The expression patterns of the auxin-responsive gene DR5:b-glucuronidase and the cytodifferentiation marker gene SCARECROW suggest that the rpd1 mutation interferes with neither axis formation nor cellular patterning at the initial stage of root primordium development. Taken together with the effect of the rpd1 mutation on callus cell proliferation, these data imply a role for RPD1 in prearranging the maintenance of the active cell proliferation during root primordium development. Positional cloning of the RPD1 gene revealed that it encodes a member of a novel protein family specific to the plant kingdom. Disruption of the RPD1 gene by a T-DNA insertion caused embryogenesis arrest at the globular to transition stages. This phenotype is consistent with the hypothesized function of RPD1 in the maintenance of active cell proliferation.The formation of adventitious and lateral roots is a typical example of de novo postembryonic organogenesis that is achieved through the elaborate regulation of cell proliferation. The process of morphogenesis common to adventitious and lateral roots can be summarized as follows. First, cell proliferation is initiated from quiescent cells in response to endogenous or external stimuli, including auxin (Boerjan et al

show abstract

“…MotA was first identified through the isolation of T4 motA 2 phages, which were shown to be defective in the expression of a set of T4 middle gene products (Mattson et al, 1974(Mattson et al, , 1978. Structural and biochemical studies have indicated that MotA contains two distinct domains: an N-terminal domain (NTD) that is formed by five a-helices and a short b-ribbon (Li et al, 2002) and houses a transcription activation function (Finnin et al, 1997;Gerber & Hinton, 1996;Pande et al, 2002) and a C-terminal domain (CTD) that by itself is capable of binding DNA (Pande et al, 2002) and is composed of a novel 'double wing' motif of three a-helices interspersed with six b-strands (Li et al, 2001). …”

mentioning

confidence: 99%

Transcriptional takeover by σ appropriation: remodelling of the σ 70 subunit of Escherichia coli RNA polymerase by the bacteriophage T4 activator MotA and co-activator AsiA

et al. 2005

View full text Add to dashboard Cite

Activation of bacteriophage T4 middle promoters, which occurs about 1 min after infection, uses two phage-encoded factors that change the promoter specificity of the host RNA polymerase. These phage factors, the MotA activator and the AsiA co-activator, interact with the s 70 specificity subunit of Escherichia coli RNA polymerase, which normally contacts the "10 and "35 regions of host promoter DNA. Like host promoters, T4 middle promoters have a good match to the canonical s 70 DNA element located in the "10 region. However, instead of the s 70 DNA recognition element in the promoter's "35 region, they have a 9 bp sequence (a MotA box) centred at "30, which is bound by MotA. Recent work has begun to provide information about the MotA/AsiA system at a detailed molecular level. Accumulated evidence suggests that the presence of MotA and AsiA reconfigures protein-DNA contacts in the upstream promoter sequences, without significantly affecting the contacts of s 70 with the "10 region. This type of activation, which is called 's appropriation', is fundamentally different from other well-characterized models of prokaryotic activation in which an activator frequently serves to force s 70 to contact a less than ideal "35 DNA element. This review summarizes the interactions of AsiA and MotA with s 70 , and discusses how these interactions accomplish the switch to T4 middle promoters by inhibiting the typical contacts of the C-terminal region of s 70 , region 4, with the host "35 DNA element and with other subunits of polymerase. OverviewUpon infection of Escherichia coli, bacteriophage T4 establishes its own developmental cycle. Within 20 min, the phage programmes the generation of approximately 200 copies of its genome, the packaging of that DNA, and finally its escape from the host by lysis (reviewed by Miller et al., 2003). Regulation of this cycle is achieved largely by phage promoters, which sequentially express early, middle and late phage genes. Because T4 does not encode its own RNA polymerase, it must direct the host transcriptional machinery to these phage promoters at the correct time during infection. T4 encodes factors that accomplish this takeover by altering the specificity of the host E. coli RNA polymerase as infection proceeds (reviewed by Miller et al., 2003;Stitt & Hinton, 1994).E. coli RNA polymerase consists of a core of five subunits (a 2 , b, b9 and v), which contains the RNA-synthesizing activity, and a s factor that binds to a specific promoter sequence and sets the start site for transcription (reviewed by Gruber & Gross, 2003;Paget & Helmann, 2003 and a 235 element, having a consensus sequence of 59-TTGACA-39 (Campbell et al., 2002;Gardella et al., 1989;Keener & Nomura, 1993;Murakami et al., 2002b;Siegele et al., 1989;Vassylyev et al., 2002;Waldburger et al., 1990).(All sequences are given as the top, i.e. the non-template, strand of DNA.) To a first approximation, the strength of a host promoter reflects the match between its 210 and 235 sequences and the canonical sequences for these region...

show abstract

The activation domain of the MotA transcription factor from bacteriophage T4

Cited by 41 publications

References 48 publications

The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ⁷⁰Subunit ofEscherichia coliRNA Polymerase

The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ⁷⁰Subunit ofEscherichia coliRNA Polymerase

A Novel Plant-Specific Family Gene, ROOT PRIMORDIUM DEFECTIVE 1, Is Required for the Maintenance of Active Cell Proliferation

Transcriptional takeover by σ appropriation: remodelling of the σ 70 subunit of Escherichia coli RNA polymerase by the bacteriophage T4 activator MotA and co-activator AsiA

Contact Info

Product

Resources

About

The activation domain of the MotA transcription factor from bacteriophage T4

Cited by 41 publications

References 48 publications

The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase

The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ70Subunit ofEscherichia coliRNA Polymerase

A Novel Plant-Specific Family Gene, ROOT PRIMORDIUM DEFECTIVE 1, Is Required for the Maintenance of Active Cell Proliferation

Transcriptional takeover by σ appropriation: remodelling of the σ 70 subunit of Escherichia coli RNA polymerase by the bacteriophage T4 activator MotA and co-activator AsiA

Contact Info

Product

Resources

About

The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ⁷⁰Subunit ofEscherichia coliRNA Polymerase

The Bacteriophage T4 Transcription Activator MotA Interacts with the Far-C-Terminal Region of the σ⁷⁰Subunit ofEscherichia coliRNA Polymerase