YY1 Binds Five cis-Elements and Trans-activates the Myeloid Cell-restricted gp91 Promoter

Jacobsen, Britta M.; Skalnik, David G.

doi:10.1074/jbc.274.42.29984

Cited by 32 publications

(26 citation statements)

References 57 publications

(71 reference statements)

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“…Interestingly, binding activities of both CBF/NF-Y and YY1 may be inhibited independently by direct interaction with the Y-Box binding protein, YB-1 (47). During terminal differentiation of myeloid cells, YY1 transactivates the gp91 phox promoter by competing with the CCAAT displacement protein (48). These findings suggest possible mechanisms by which YY1 may function to release the promoter from inhibition by the upstream factor.…”

Section: Discussionmentioning

confidence: 78%

YY1 Is a Positive Regulator of Transcription of theCol1a1 Gene

Riquet

Tan

Choy

et al. 2001

Journal of Biological Chemistry

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Both cell-specific and ubiquitous transcription factors in fibroblasts have been identified as critical for expression of the Col1a1 gene, which encodes the ␣1 chain of type I collagen. Here, we report that Yin Yang 1 (YY1) binds to the Col1a1 promoter immediately upstream of the TATA box, and we examine the functional implications of YY1 binding for regulation of Col1a1 gene expression in BALBc/3T3 fibroblasts. The Col1a1 promoter region spanning base pairs (bp) -56 to -9 bound purified recombinant YY1 and the corresponding binding activity in nuclear extracts was supershifted using a YY1-specific antibody. Mutation of the TATA box to TgTA enhanced YY1 complex formation. Mutation analysis revealed two YY1 core binding sites at -40/-37 bp (YY1A) and, on the reverse strand, at -32/-29 bp (YY1B) immediately adjacent to the TATA box. In transfections using Col1a1-luciferase constructs, mutation of YY1A decreased activity completely (wild-type p350 (p350wt), -222/؉113 bp) or partially (p130wt, -84 bp/؉13 bp), whereas mutation of YY1B blocked the expression of both promoter constructs. Cotransfection with pCMV-YY1 increased p350wt and p130wt activities by as much as 10-fold, whereas antisense YY1 decreased constitutive expression and blocked the increased activity due to pCMV-YY1 overexpression. The mTgTA constructs were devoid of activity, arguing for a requirement for cognate binding of the TATA box-binding protein (TBP). Electrophoretic mobility shift assays performed under conditions permitting TBP binding showed that recombinant TBP/TFIID and YY1 could bind to the -56/-9 bp fragment and that YY1B was the preferred site for YY1 binding. Our results indicate that YY1 binds to the Col1a1 proximal promoter and functions as a positive regulator of constitutive activity in fibroblasts. Although YY1 is not sufficient for transcriptional initiation, it is a required component of the transcription machinery in this promoter.

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Section: Discussionmentioning

confidence: 78%

YY1 Is a Positive Regulator of Transcription of theCol1a1 Gene

Riquet

Tan

Choy

et al. 2001

Journal of Biological Chemistry

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“…Binding of the transcription factor YY1 to two YY1-binding sites in the proximal promoter was detected and shown to increase Nox2 promoter activity in vitro. However, the function of YY1 during myeloid cell development is not clear because YY1 protein levels do not correlate with differentiation and Nox2 expression [120]. Co-treatment with IFN-γ and LPS strongly activates Nox2 expression in phagocytes.…”

Section: B Regulation Of Nox2 Expressionmentioning

confidence: 99%

Regulation of Nox and Duox enzymatic activity and expression

Lambeth

Kawahara

Diebold

2007

Free Radical Biology and Medicine

452

422

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SummaryIn recent years, it has become clear that reactive oxygen species (ROS, which include superoxide, hydrogen peroxide and other metabolites) are produced in biological systems. Rather than being simply a byproduct of aerobic metabolism, it is now recognized that specific enzymes ---the Nox (NADPH-oxidase) and Duox (Dual oxidase) enzymes ----seem to have the sole function of generating ROS in a carefully regulated manner, and key roles in signal transduction, immune function, hormone biosynthesis and other normal biological functions are being uncovered. The prototypical Nox is the respiratory burst oxidase or phagocyte oxidase, which generates large amounts of superoxide and other reactive species in the phagosomes of neutrophils and macrophages, playing a central role in innate immunity by killing microbes. This enzyme system has been extensively studied over the past two decades, and provides a basis for comparison with the more recently described Nox and Duox enzymes, which generate ROS in a variety of cells and tissues. This review first considers the structure and regulation of the respiratory burst oxidase, and then reviews recent studies relating to the regulation of the activity of the novel Nox/Duox enzymes. The regulation of Nox and Duox expression in tissues and by specific stimuli is also considered here. An accompanying review considers biological and pathological roles of the Nox family of enzymes. The Respiratory Burst Oxidase of Phagocytes a. The respiratory burstThe "respiratory burst" refers to the early observation that when professional phagocytes such as neutrophils and macrophages are exposed to microbes, they consume large amounts of oxygen. Unexpectedly, this oxygen consumption was not inhibited by cyanide, an inhibitor of mitochondrial electron transport. This observation led to a more than 25 year search for the enzymatic origin of the respiratory burst and to the eventual discovery and molecular characterization of the phagocytic NADPH-oxidase or "respiratory burst oxidase". The phagocyte oxidase generates superoxide via the one electron-reduction of oxygen by NADPH, with secondary production of hydrogen peroxide, HOCl and other activated forms of oxygen. Together, these reactive oxygen species (ROS) participate in host defense by killing invading microbes. b. gp91 phox , the catalytic moiety of the respiratory burst oxidaseThe phagocytic NADPH-oxidase consists of a membrane-localized glycosylated, catalytic subunit, gp91 phox (which has also come to be known as Nox2, a terminology that will be used in this review), along with a second membrane-associated subunit, p22 phox , both depicted in Fig. 1. Nox2 and p22 phox stabilize one another in a tightly associated heterodimer which is referred to as flavocytochrome b 558 . The C-terminal half of Nox2 forms a domain that is Contact information: 148 Whitehead Biomedical Research Building, Department of Pathology and Laboratory Medicine, 615 Michael Street, Atlanta, GA 30322, U.S. A. Phone: 404-727-5875, Fax: 404-712-2979, e-mail: nox...

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“…These include the repressors SATB1, CDP, and HoxA10 (5, 7, 52) and the activators YY1, CP1, GATA-1, GATA-2, IRF-1, and IRF-2 (5,7,16,17,21). Interaction and/or competition between these factors presumably plays a role in appropriate gp91 phox regulation.…”

Section: Satb1 Represses Gp91mentioning

confidence: 99%

“…All CDP-binding site oligonucleotides derived from the human gp91 phox promoter are as described previously (5)(6)(7)16). Numbers refer to the nucleotide position within the human gp91 phox promoter (5).…”

Section: Fig 2 Cdp and Satb1 Interact With Multiple Elements Withinmentioning

confidence: 99%

The Matrix Attachment Region-binding Protein SATB1 Interacts with Multiple Elements within the gp91 Promoter and Is Down-regulated during Myeloid Differentiation

Hawkins¹,

Kohwi‐Shigematsu²,

Skalnik³

2001

Journal of Biological Chemistry

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The gp91phox gene encodes a component of the respiratory burst NADPH oxidase complex and is highly expressed in mature myeloid cells. The transcriptional repressor CCAAT displacement protein binds to at least five sites within the proximal gp91 phox promoter and represses expression prior to terminal phagocyte differentiation. The DNA binding activity of CCAAT displacement protein decreases during terminal phagocyte differentiation, thus permitting the binding of transcriptional activators and induction of gp91 phox expression. We report here that the matrix attachment region-binding protein SATB1 interacts with at least seven sites within the ؊1542 to ؉12-base pair gp91 phox promoter. Four additional binding sites for CCAAT displacement protein were also identified. Furthermore, the most proximal SATB1-binding site within the gp91 phox promoter binds specifically to the nuclear matrix fraction in vitro. SATB1 expression is downregulated during terminal myeloid cell differentiation, coincident with induction of gp91 phox expression. Transient transfection assays demonstrate that a SATB1-binding site derived from the gp91 phox promoter represses promoter activity in cells expressing SATB1. These findings underscore the importance of transcriptional repression in the regulation of gp91 phox expression and reveal a candidate myeloid cell target gene for SATB1, a factor previously found to be essential for T cell development.

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YY1 Binds Five cis-Elements and Trans-activates the Myeloid Cell-restricted gp91 Promoter

Cited by 32 publications

References 57 publications

YY1 Is a Positive Regulator of Transcription of theCol1a1 Gene

YY1 Is a Positive Regulator of Transcription of theCol1a1 Gene

Regulation of Nox and Duox enzymatic activity and expression

The Matrix Attachment Region-binding Protein SATB1 Interacts with Multiple Elements within the gp91 Promoter and Is Down-regulated during Myeloid Differentiation

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