The Novel Mrf-2 DNA-Binding Domain Recognizes a Five-Base Core Sequence through Major and Minor-Groove Contacts

Whitson, Robert H.; Huang, Ting‐Hsiang; Itakura, Keiichi

doi:10.1006/bbrc.1999.0643

Cited by 51 publications

(57 citation statements)

References 16 publications

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“…DRI binds to a core ATTA motif similar to that present in homeodomain sites (9). MRF-2 binds preferentially to the sequence AATAC/T in binding site selection assays (43). While the properties of these proteins have suggested that ARIDs have intrinsic specificity for AT-rich sequences (albeit of somewhat different compositions), analysis of p270 indicates that sequence specificity is not intrinsic to the core ARID motif.…”

mentioning

confidence: 99%

The Human SWI-SNF Complex Protein p270 Is an ARID Family Member with Non-Sequence-Specific DNA Binding Activity

Dallas

Pacchione

Wilsker

et al. 2000

Molecular and Cellular Biology

112

100

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p270 is an integral member of human SWI-SNF complexes, first identified through its shared antigenic specificity with p300 and CREB binding protein. The deduced amino acid sequence of p270 reported here indicates that it is a member of an evolutionarily conserved family of proteins distinguished by the presence of a DNA binding motif termed ARID (AT-rich interactive domain). The ARID consensus and other structural features are common to both p270 and yeast SWI1, suggesting that p270 is a human counterpart of SWI1. The approximately 100-residue ARID sequence is present in a series of proteins strongly implicated in the regulation of cell growth, development, and tissue-specific gene expression. Although about a dozen ARID proteins can be identified from database searches, to date, only Bright (a regulator of B-cell-specific gene expression), dead ringer (a Drosophila melanogaster gene product required for normal development), and MRF-2 (which represses expression from the cytomegalovirus enhancer) have been analyzed directly in regard to their DNA binding properties. Each binds preferentially to AT-rich sites. In contrast, p270 shows no sequence preference in its DNA binding activity, thereby demonstrating that AT-rich binding is not an intrinsic property of ARID domains and that ARID family proteins may be involved in a wider range of DNA interactions.SWI-SNF complexes were first identified in yeast cells, where they are involved in the regulation of an array of inducible genes including those required for the mating type switch and sucrose fermentation pathways (16, 28). More-recent studies suggest that these complexes have a more general role in the regulation of gene expression. The isolation and characterization of Drosophila melanogaster and mammalian homologs of many of the yeast complex members suggest that SWI-SNF complexes play fundamental roles in the regulation of gene expression during cell growth and development in all organisms (reviewed in reference 14; 17).Although SWI-SNF complexes have demonstrated DNA binding capabilities (29), the source of this activity in the complexes remains unclear. The only DNA binding protein identified to date in mammalian SWI-SNF complexes is BAF-57, which has a DNA binding activity restricted to four-way junction DNA. SWI-SNF complexes lacking a functional BAF-57 retain DNA binding activity, indicating that other DNA binding components must be present (41).p270 is an integral member of human SWI-SNF complexes, first identified through its shared antigenic specificity with p300 and CREB binding protein (CBP) (5, 6). The p300/CBP/p270 cross-reactive antibodies coprecipitate a series of proteins that includes the mammalian SWI-SNF complex components BRG1, BAF-170, BAF-155, and hSNF5/Ini1. Conversely, antibodies directed against the individual human SWI-SNF complex components BRG1 and BAF-155 immunoprecipitate p270, as demonstrated by reactivity with a p270-specific antibody (6). The sequence of p270 described here indicates that this protein contains a highly conserved...

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confidence: 99%

The Human SWI-SNF Complex Protein p270 Is an ARID Family Member with Non-Sequence-Specific DNA Binding Activity

Dallas

Pacchione

Wilsker

et al. 2000

Molecular and Cellular Biology

112

100

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“…2) (27). The binding sites of the ARID3 subfamily Bright and DRI and ARID5 subfamily MRF2 are (A/G)AT(T/A)AA, (A/G)ATTAA or TATTGAT, and AATA(C/T), respectively (28,29,31,32). These sequences contain ATT or AT/ATC runs.…”

Section: Discussionmentioning

confidence: 99%

“…The Bright core binding sites also flanked with AT or ATC run containing AT dimers, which are characteristic of matrix attachment region recognition sites (28). The binding site of the ARID5 subfamily MRF2 is AATA(C/T) (32). Some ARID family proteins are not sequence-specific DNA-binding proteins or they do not bind AT-rich sequences (26,27).…”

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confidence: 99%

A Novel ARID/Bright-like Protein Involved in Transcriptional Activation of Cyst Wall Protein 1 Gene in Giardia lamblia

Wang

Sun

2007

Journal of Biological Chemistry

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The capability of protozoan parasite Giardia lamblia to encyst is critical for survival outside the host and its transmission. AT-rich interaction domain (ARID) or Bright homologs constitute a large family of transcription factors in higher eukaryotes that regulate cell proliferation, development, and differentiation. We asked whether Giardia has ARID-like genes and whether they influence gene expression during Giardia encystation. Blast searches of the Giardia genome data base identified two genes with putative ARID/Bright domains (gARID1 and 2). Epitope-tagged gARID1 was found to localize to nuclei. Recombinant gARID1 specifically bound to the encystation-induced cyst wall protein (cwp) gene promoters. Mutation analysis revealed that AT-rich initiators were required for binding of gARID1 to the cwp promoters. gARID1 contains several key residues for DNA binding, and its binding sequences are similar to those of the known ARID family proteins. The gARID1 binding sequences were positive cis-acting elements of the cwp1 promoter during both vegetative growth and encystation. We also found that gARID1 transactivated the cwp1 promoter through its binding sequences in vivo. Our results suggest that the ARID family has been conserved during evolution and that gARID1 is an important transactivator in regulation of the Giardia cwp1 gene, which is key to Giardia differentiation into cysts.Giardia lamblia is an important human intestinal parasite that causes outbreaks of waterborne diarrheal disease (1, 2). It has two life cycle stages that are well adapted to survival in different inhospitable environments (3-6). The motile flagellated trophozoites attach to and colonize the human small intestine to cause the symptoms of giardiasis. The dormant infective cysts, which are protectively walled and resistant to external hostile conditions, are responsible for transmission of giardiasis.The ability of trophozoites to encyst in the intestine is key to Giardia pathophysiology. However, little is known of the regulation of encystation. Synthesis and secretion of specific proteins and polysaccharide required for the formation of a protective cyst wall is a major process of encystation (3, 5-7). Expression of genes encodes three cyst wall structural proteins (Cwp1, Cwp2, Cwp3) (8 -10), and glucosamine-6-phosphate isomerase-B, the first enzyme in the cyst wall polysaccharide biosynthetic pathway (11, 12), increases with similar kinetics during encystation (6, 9, 11, 12), suggesting the importance of regulation at the transcriptional level.G. lamblia is of significant evolutionary interest because it has been proposed as one of the most early diverging eukaryotes (13,14). The giardial transcription mechanism may be unusual because relatively short 5Ј-flanking regions (Ͻ65 bp) are sufficient for the expression of many constitutive and encystationinduced giardial genes (11,(15)(16)(17). No classical TATA or CCAAT boxes or other cis-acting elements have been found in the promoters of many giardial protein-coding genes (16, 18). AT-rich...

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“…It was identified in our laboratory in 1996 as a novel nuclear protein that binds to sequences upstream of the human cytomegalovirus major immediate-early enhancer/promoter and exerts repressor activity in undifferentiated human Tera-2 cells (1). Subsequent studies revealed the three-dimensional structure of the novel DNA-binding motif (ARID) of Mrf-2 and mechanisms of DNA recognition (2)(3)(4). The ARID family of DNA-binding proteins has grown since then to include fifteen proteins found in humans and most other vertebrate species, and six proteins found in Drosophila as well as proteins found in worms, fungi, plants and yeast (5)(6)(7)(8).…”

Section: Arid5b (At-rich Interaction Domain-containingmentioning

confidence: 99%

Knockdown of AT-rich interaction domain (ARID) 5B gene expression induced AMPKα2 activation in cardiac myocytes

Hirose-Yotsuya

Okamoto

Yamakawa

et al. 2015

BST

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The Novel Mrf-2 DNA-Binding Domain Recognizes a Five-Base Core Sequence through Major and Minor-Groove Contacts

Cited by 51 publications

References 16 publications

The Human SWI-SNF Complex Protein p270 Is an ARID Family Member with Non-Sequence-Specific DNA Binding Activity

The Human SWI-SNF Complex Protein p270 Is an ARID Family Member with Non-Sequence-Specific DNA Binding Activity

A Novel ARID/Bright-like Protein Involved in Transcriptional Activation of Cyst Wall Protein 1 Gene in Giardia lamblia

Knockdown of AT-rich interaction domain (ARID) 5B gene expression induced AMPKα2 activation in cardiac myocytes

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