Precise nucleosome positioning in the promoter of the chicken<i>β</i><sup>A</sup>globin gene

Kefalas, Panagiotis; Gray, Fiona C.; Allan, James

doi:10.1093/nar/16.2.501

Cited by 19 publications

(14 citation statements)

References 20 publications

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“…5) translational frame occupied by an in vitro-positioned nucleosome (27) reveals that the suGF1 recognition site lies entirely within and close to the dyad of the positioned nucleosome. The binding site for BGP1 on the PA-globin promoter also occurs within an in vitro-positioned nucleosome, although in this case the G string occurs near the border of the positioned nucleosome, where the DNAhistone interactions may be relatively weak (18). These results are summarized in Fig.…”

Section: Figmentioning

confidence: 86%

Purification of an oligo(dG).oligo(dC)-binding sea urchin nuclear protein, suGF1: a family of G-string factors involved in gene regulation during development.

Hapgood¹,

Patterton²

1994

Mol. Cell. Biol.

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Genes Dev.2: [863][864][865][866][867][868][869][870][871][872][873] 1988). We have purified a 59.5-kDa nuclear protein (suGF1) from sea urchin embryos by DNA affinity chromatography. suGF1 has high binding affinity and specificity for oligo(dG) -oligo(dC). The identity of the purified protein was confirmed by renaturation of sequence-specific DNA-binding activity from a sodium dodecyl sulfate-polyacrylamide gel slice and by Southwestern (DNA-protein) (4,19). In addition, G-string-binding factors have been detected in a number of different tissues from various organisms (8,19,22,38). The promoter of the chicken adult 3-globin gene contains a G string of 16 to 18 Gs (22, 28). There is strong evidence that regulation of expression of this gene involves a complex interplay between binding of a G-string factor, DNA conformation, and displacement of a positioned nucleosome at the G string (22). A G6 string has also been implicated in regulation of gene expression during sea urchin development via binding of a G-string factor to a cis-regulatory element present in the promoter of a cell lineage-specific gene LpS13 (38). This sea urchin G-string factor may be related to a putative mammalian transcription factor, IF1, implicated in the coordinate regulation of expression of the (xl (I) and a2 (I) collagen genes during embryonic development via binding to G7 strings present in both promoters (17, 38). Interestingly, a G7 string occurs within a purine-rich region of the chicken ct2(I) collagen gene promoter which is hypersensitive to Si nuclease and DNase I in chromatin in a tissuespecific fashion (24).G strings have in common with homopurine-homopyrimidine (pur. pyr) stretches the ability to form unusual DNA structures such as triple helices in vitro, the formation of which depends critically on the degree of superhelical stress of the DNA, the length of the homopurine stretch, and the chemical environment (21,36). Several authors have proposed that G strings may function in vivo as a conformational switch which is modulated in some way by G-stringbinding proteins (4,19,20,24).A similar role has been proposed for G-rich regions which occur within pur. pyr stretches upstream of several housekeeping genes such as the c-Ki-ras, epidermal growth factor receptor, and c-myc genes (6,12,14,23,29). These pur-pyr regions are S1 nuclease sensitive in vitro and bind to factors containing multiple copies of the sequence GGGNGGG in their DNA recognition sites. In some cases, alterations in chromatin structure correlating with the state of expression of these genes have been mapped to the pur. pyr regions in nuclei.These observations raise several unresolved issues. G strings may play a role in gene regulation during development via families of G-string factors with related functions. The structural and functional relationships among various G-string factors as well as factors binding to G-rich sequences within pur-pyr stretches need to be examined, considering the parallels that can be drawn between their proposed biological role...

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Section: Figmentioning

confidence: 86%

Purification of an oligo(dG).oligo(dC)-binding sea urchin nuclear protein, suGF1: a family of G-string factors involved in gene regulation during development.

Hapgood¹,

Patterton²

1994

Mol. Cell. Biol.

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“…Regions of the chicken f3A-globin promoter to which proteins bind. G-string, 16 consecutive dG residues; Spl, a weak Spi site at the 3' end of the G-string; Pal, partially palindromic sequence to which the PAL factor binds (3,6); CACCC, f3-globin consensus sequence (4,30); Y, polypyrimidine stretch; R, polypurine stretch, to which the factor NFE-4 binds (33). Spl binds weakly to the 3' end of the G-string, with moderate affinity to the CACCC and polypyrimidine sequences, and with relatively higher affinity to the polypurine tract (1,32).…”

Section: Dna Binding Measurementsmentioning

confidence: 99%

“…Such binding might directly affect nucleosome positioning near the A-globin promoter. Furthermore, it has been suggested (24,28,29) that the interconversion of the G-string between B-and H-(or other non-B) form DNA is an important regulatory mechanism either directly in control of transcription or indirectly through alteration in nucleosome position or conformation (30). The binding of BGPI would certainly play a role in such an interconversion process.…”

Section: Dba4mmentioning

confidence: 99%

Properties of BGP1, a poly(dG)-binding protein from chicken erythrocytes

1990

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The chicken beta A-globin gene contains in the neighborhood of its 5' promoter a (dG)-homopolymer sequence 16 base pairs long. The 66 kD protein BGP1 (beta globin protein 1), isolated from chicken erythrocytes, has been shown to bind specifically to this sequence. We describe further purification of BGP1, measure its affinity for the beta A-globin promoter binding site, and analyze its binding properties. The minimal binding sequence is seven dG residues; methylation interference studies show that each of these residues contacts BGP1. Binding competition experiments employing (dG).(dC) oligomers of varying lengths also consistent with (dG)7 as a minimum recognition sequence. All of the data can be explained by a model in which BGP1 binds to any contiguous set of seven (dG) residues, so that the effective constant for binding to (dG)n is proportional to n minus 6. This behavior may be typical of proteins that bind specifically to repeated sequences.

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“…The role we tentatively propose for BGPl has not been demonstrated. However, nucleosome phasing observed in inactive cells in vivo appears to be reconstructible in vitro with cloned promoter DNA fragments and purified histones (Kefalas et al 1988). With the purification of BGPl (S. Clark, unpubl.)…”

Section: The Role Of Bgplmentioning

confidence: 99%

An erythrocyte-specific protein that binds to the poly(dG) region of the chicken beta-globin gene promoter.

Lewis¹,

Clark²,

Felsenfeld³

et al. 1988

Genes Dev.

104

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The promoter region of the chicken aduh p-globin gene contains a sequence of 16 deoxyguanosine residues located at a nucleosome boundary in tissues where the gene is inactive. In definitive erythrocytes that express the p-globin gene, the nucleosome is displaced, the G-string and adjacent sequences are occupied by sequencespecific DNA-binding proteins, and a nuclease hypersensitive domain is generated in this region. To gain insight into the role of the G-string in this series of events, we have examined the proteins that bind to it. Using the gel mobility shift assay and a monoclonal antibody that blocks specific binding to the G-string, we have identified a specific protein, BGPl, that is found only in chicken erythroid cells and appears at the same time, or shortly before, the changes in chromatin structure. The antibody interacts strongly with BGPl and cross-reacts weakly with Spl. Although both BGPl and Spl require Zn^+ for their DNA-binding activity, these proteins differ in their binding-site specificities, chromatographic properties, and molecular weights. In contrast to Spl, which is found in a wide variety of cell types, BGPl is restricted to erythrocytes and is most abundant in definitive erythrocytes. Thus, its presence corresponds to the tissue-and stage-specific occupancy of the G-string in vivo.

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Precise nucleosome positioning in the promoter of the chickenβ^Aglobin gene

Cited by 19 publications

References 20 publications

Purification of an oligo(dG).oligo(dC)-binding sea urchin nuclear protein, suGF1: a family of G-string factors involved in gene regulation during development.

Purification of an oligo(dG).oligo(dC)-binding sea urchin nuclear protein, suGF1: a family of G-string factors involved in gene regulation during development.

Properties of BGP1, a poly(dG)-binding protein from chicken erythrocytes

An erythrocyte-specific protein that binds to the poly(dG) region of the chicken beta-globin gene promoter.

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Precise nucleosome positioning in the promoter of the chickenβAglobin gene

Cited by 19 publications

References 20 publications

Purification of an oligo(dG).oligo(dC)-binding sea urchin nuclear protein, suGF1: a family of G-string factors involved in gene regulation during development.

Purification of an oligo(dG).oligo(dC)-binding sea urchin nuclear protein, suGF1: a family of G-string factors involved in gene regulation during development.

Properties of BGP1, a poly(dG)-binding protein from chicken erythrocytes

An erythrocyte-specific protein that binds to the poly(dG) region of the chicken beta-globin gene promoter.

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Precise nucleosome positioning in the promoter of the chickenβ^Aglobin gene