Characterization of the chromatin structure in the upstream region of the chicken alpha-globin gene domain

1994 ◽  
Vol 242 (6) ◽  
pp. 649-652 ◽  
Author(s):  
S. V. Razin ◽  
C. V. De Moura Gallo ◽  
K. Scherrer
Keyword(s):  
Chromatin Structure ◽  
Globin Gene ◽  
Upstream Region ◽  
Alpha Globin ◽  
Globin Gene Domain

scholarly journals Characterization of DNA sequences localized 11 to 17.5 kb upstream of the chicken embryonic pi-globin gene.

1999 ◽  
Vol 46 (3) ◽  
pp. 777-784
Author(s):  
M Pietrowska ◽  
M Rusin ◽  
P Widłak ◽  
S V Razin ◽  
J Rzeszowska-Wolny
Keyword(s):  
Dna Sequences ◽  
Globin Gene ◽  
Matrix Proteins ◽  
Inverted Repeats ◽  
Nuclear Matrix Proteins ◽  
Alpha Globin ◽  
Dna Fragment ◽  
Globin Gene Domain

We have analyzed the DNA fragment localized about 11 to 17.5 kb upstream of the chicken alpha-globin gene domain (the fragment was designed as alpha-0). The nucleotide sequence of its 3.3 kb-long 5' part was established and interactions with nuclear matrix proteins were studied. The DNA region localized about 16 kb upstream of the embryonic pi-globin gene showed high affinity to nuclear matrices in vitro. Two palindromes and a cluster of inverted repeats were co-localized in the same region. The whole 6.6 kb alpha-0 fragment decreased the activity of linked CAT reporter gene when transfected into chicken erythroblastoid cells.

Characterization of the major regulatory element upstream of the human alpha-globin gene cluster

1991 ◽  
Vol 11 (9) ◽  
pp. 4679-4689
Author(s):  
A P Jarman ◽  
W G Wood ◽  
J A Sharpe ◽  
G Gourdon ◽  
H Ayyub ◽  
...  
Keyword(s):  
Regulatory Element ◽  
Globin Gene ◽  
Major Elements ◽  
Beta Globin ◽  
Globin Mrna ◽  
Expression Studies ◽  
Primary Element ◽  
Alpha Globin ◽  
Binding Sequence

The major positive regulatory activity of the human alpha-globin gene complex has been localized to an element associated with a strong erythroid-specific DNase I hypersensitive site (HS -40) located 40 kb upstream of the zeta 2-globin mRNA cap site. Footprint and gel shift analyses of the element have demonstrated the presence of four binding sites for the nuclear factor GATA-1 and two sites corresponding to the AP-1 consensus binding sequence. This region resembles one of the major elements of the beta-globin locus control region in its constitution and characteristics; this together with evidence from expression studies suggests that HS -40 is a primary element controlling alpha-globin gene expression.

scholarly journals Chromatin structure and developmental expression of the human alpha-globin cluster.

1986 ◽  
Vol 6 (4) ◽  
pp. 1108-1116 ◽  
Author(s):  
M Yagi ◽  
R Gelinas ◽  
J T Elder ◽  
M Peretz ◽  
T Papayannopoulou ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Chromatin Structure ◽  
Bone Marrow Cells ◽  
Fetal Liver ◽  
Globin Gene ◽  
Erythroid Cells ◽  
Adult Bone Marrow ◽  
Hypersensitive Sites ◽  
Alpha Globin ◽  
Adult Bone

The human alpha-like globins undergo a switch from the embryonic zeta-chain to the alpha-chain early in human development, at approximately the same time as the beta-like globins switch from the embryonic epsilon-to the fetal gamma-chains. We investigated the chromatin structure of the human alpha-globin gene cluster in fetal and adult erythroid cells. Our results indicate that DNase I-hypersensitive sites exist at the 5' ends of the alpha 1- and alpha 2-globin genes as well as at several other sites in the cluster in all erythroid cells examined. In addition, early and late fetal liver erythroid cells and adult bone marrow cells contain hypersensitive sites at the 5' end of the zeta gene, and in a purified population of 130-day-old fetal erythroid cells, the entire zeta-to alpha-globin region is sensitive to DNase I digestion. The presence of features of active chromatin in the zeta-globin region in fetal liver and adult bone marrow cells led us to investigate the transcription of zeta in these cells. By nuclear runoff transcription studies, we showed that initiated polymerases are present on the zeta-globin gene in these normal erythroid cells. Immunofluorescence with anti-zeta-globin antibodies also showed that late fetal liver cells contain zeta-globin. These findings demonstrate that expression of the embryonic zeta-globin continues at a low level in normal cells beyond the embryonic to fetal globin switch.

scholarly journals Organization of the 3′-boundary of the chicken α globin gene domain and characterization of a CR 1-specific protein binding site

1990 ◽  
Vol 18 (3) ◽  
pp. 401-409 ◽  
Author(s):  
Gabriel Farache ◽  
Sergey V. Razin ◽  
Félix Recillas Targa ◽  
Klaus Scherrer
Keyword(s):  
Protein Binding ◽  
Binding Site ◽  
Globin Gene ◽  
Specific Protein ◽  
Protein Binding Site ◽  
Globin Gene Domain

scholarly journals Identification and characterization of multiple erythroid cell proteins that interact with the promoter of the murine alpha-globin gene.

1988 ◽  
Vol 8 (8) ◽  
pp. 3215-3226 ◽  
Author(s):  
K M Barnhart ◽  
C G Kim ◽  
S S Banerji ◽  
M Sheffery
Keyword(s):  
Transcription Factor ◽  
Binding Site ◽  
Binding Sites ◽  
Globin Gene ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Erythroid Cell ◽  
Alpha Globin ◽  
Murine Erythroleukemia

The proteins responsible for erythroid-specific footprints extending to -180 on the mouse alpha-globin gene were identified, enriched, and characterized from extracts of murine erythroleukemia (MEL) cells. Three proteins accounted for most aspects of the footprints. The binding sites of two proteins, termed alpha-CP1 and alpha-CP2, overlapped in the CCAAT box. Further characterization of these two CCAAT binding proteins showed that neither interacted with the adenovirus origin of replication, a strong CCAAT transcription factor-nuclear factor 1 binding site. A third protein, termed alpha-IRP, interacted with two sequences that formed an inverted repeat (IR) between the CCAAT and TATAA boxes. Interestingly, the binding domain of one of the CCAAT factors, alpha-CP1, overlapped one alpha-IRP binding site. alpha-CP1 thus overlapped the binding domains of both alpha-CP2 and alpha-IRP. The IRs included GC-rich sequences reminiscent of SP1-binding sites. Indeed, alpha-IRP bound as well to the alpha-promoter as it did to SP1 sites in the simian virus 40 early promoter. These results suggest that alpha-IRP may be related to the transcription factor Sp1. We determined the level of each alpha-globin-binding activity before and after induced erythroid differentiation of MEL cells. We found that differentiation caused alpha-CP1 activity to drop three- to fivefold, while alpha-IRP activity decreased slightly and alpha-CP2 activity increased two- to threefold.

Identification and characterization of multiple erythroid cell proteins that interact with the promoter of the murine alpha-globin gene

1988 ◽  
Vol 8 (8) ◽  
pp. 3215-3226
Author(s):  
K M Barnhart ◽  
C G Kim ◽  
S S Banerji ◽  
M Sheffery
Keyword(s):  
Transcription Factor ◽  
Binding Site ◽  
Binding Sites ◽  
Globin Gene ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Erythroid Cell ◽  
Alpha Globin ◽  
Murine Erythroleukemia

The proteins responsible for erythroid-specific footprints extending to -180 on the mouse alpha-globin gene were identified, enriched, and characterized from extracts of murine erythroleukemia (MEL) cells. Three proteins accounted for most aspects of the footprints. The binding sites of two proteins, termed alpha-CP1 and alpha-CP2, overlapped in the CCAAT box. Further characterization of these two CCAAT binding proteins showed that neither interacted with the adenovirus origin of replication, a strong CCAAT transcription factor-nuclear factor 1 binding site. A third protein, termed alpha-IRP, interacted with two sequences that formed an inverted repeat (IR) between the CCAAT and TATAA boxes. Interestingly, the binding domain of one of the CCAAT factors, alpha-CP1, overlapped one alpha-IRP binding site. alpha-CP1 thus overlapped the binding domains of both alpha-CP2 and alpha-IRP. The IRs included GC-rich sequences reminiscent of SP1-binding sites. Indeed, alpha-IRP bound as well to the alpha-promoter as it did to SP1 sites in the simian virus 40 early promoter. These results suggest that alpha-IRP may be related to the transcription factor Sp1. We determined the level of each alpha-globin-binding activity before and after induced erythroid differentiation of MEL cells. We found that differentiation caused alpha-CP1 activity to drop three- to fivefold, while alpha-IRP activity decreased slightly and alpha-CP2 activity increased two- to threefold.

Mapping of structural and transcription-related matrix attachment sites in the alpha-globin gene domain of avian erythroblasts and erythrocytes

1990 ◽  
Vol 10 (10) ◽  
pp. 5349-5358
Author(s):  
G Farache ◽  
S V Razin ◽  
J Rzeszowska-Wolny ◽  
J Moreau ◽  
F R Targa ◽  
...  
Keyword(s):  
Nuclear Matrix ◽  
Large Fraction ◽  
Globin Gene ◽  
Dna Interaction ◽  
Globin Genes ◽  
Origin Of Replication ◽  
Attachment Sites ◽  
Alpha Globin ◽  
Globin Gene Domain ◽  
Structural Matrix

The positions of preferential DNA interaction with the nuclear matrix were mapped within the domain of the chicken alpha-globin genes in transcriptionally active erythroblast nuclei and inactive nuclei of mature erythrocytes. In the latter, only two major distinct attachment sites were observed, close to the A + T-rich sequences previously found at the boundaries of the domain. Sequencing of these structural matrix attachment points revealed several known DNA motifs; some of them were present on both sides of the domain. In actively transcribing erythroblast nuclei of adult animals, a large fraction of the transcribed area was represented in nuclear matrix DNA, including upstream and downstream elements. In particular, adult alpha A- and alpha D-globin genes were found in matrix DNA, while the transcribed but translationally unexpressed embryonic pi gene was underrepresented. The data are discussed in terms of the existence of stable or structural and expression-related matrix attachment sites; correlations to the origin of replication and the units of transcription of the domain are shown.

Chromatin structure and developmental expression of the human alpha-globin cluster

1986 ◽  
Vol 6 (4) ◽  
pp. 1108-1116
Author(s):  
M Yagi ◽  
R Gelinas ◽  
J T Elder ◽  
M Peretz ◽  
T Papayannopoulou ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Chromatin Structure ◽  
Bone Marrow Cells ◽  
Fetal Liver ◽  
Globin Gene ◽  
Erythroid Cells ◽  
Adult Bone Marrow ◽  
Hypersensitive Sites ◽  
Alpha Globin ◽  
Adult Bone

The human alpha-like globins undergo a switch from the embryonic zeta-chain to the alpha-chain early in human development, at approximately the same time as the beta-like globins switch from the embryonic epsilon-to the fetal gamma-chains. We investigated the chromatin structure of the human alpha-globin gene cluster in fetal and adult erythroid cells. Our results indicate that DNase I-hypersensitive sites exist at the 5' ends of the alpha 1- and alpha 2-globin genes as well as at several other sites in the cluster in all erythroid cells examined. In addition, early and late fetal liver erythroid cells and adult bone marrow cells contain hypersensitive sites at the 5' end of the zeta gene, and in a purified population of 130-day-old fetal erythroid cells, the entire zeta-to alpha-globin region is sensitive to DNase I digestion. The presence of features of active chromatin in the zeta-globin region in fetal liver and adult bone marrow cells led us to investigate the transcription of zeta in these cells. By nuclear runoff transcription studies, we showed that initiated polymerases are present on the zeta-globin gene in these normal erythroid cells. Immunofluorescence with anti-zeta-globin antibodies also showed that late fetal liver cells contain zeta-globin. These findings demonstrate that expression of the embryonic zeta-globin continues at a low level in normal cells beyond the embryonic to fetal globin switch.

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