Protein-DNA interactions at the H4-Site III upstream transcriptional element of a cell cycle regulated histone H4 gene: Differences in normal versus tumor cells

1992 ◽  
Vol 49 (1) ◽  
pp. 93-110 ◽  
Author(s):  
C. Willemien van der Houven van Oordt ◽  
Andre J. van Wijnen ◽  
Ruth Carter ◽  
Kenneth Soprano ◽  
Jane B. Lian ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Tumor Cells ◽  
Histone H4 ◽  
Dna Interactions ◽  
Protein Dna Interactions ◽  
A Cell ◽  
Histone H4 Gene

ATF1 and CREB Trans-Activate a Cell Cycle Regulated Histone H4 Gene at a Distal Nuclear Matrix Associated Promoter Element†

Biochemistry ◽  
1997 ◽  
Vol 36 (47) ◽  
pp. 14447-14455 ◽  
Author(s):  
Bo Guo ◽  
Janet L. Stein ◽  
André J. van Wijnen ◽  
Gary S. Stein
Keyword(s):  
Cell Cycle ◽  
Nuclear Matrix ◽  
Promoter Element ◽  
Histone H4 ◽  
A Cell ◽  
Histone H4 Gene

scholarly journals Overlapping and CpG methylation-sensitive protein-DNA interactions at the histone H4 transcriptional cell cycle domain: distinctions between two human H4 gene promoters.

1992 ◽  
Vol 12 (7) ◽  
pp. 3273-3287 ◽  
Author(s):  
A J van Wijnen ◽  
F M van den Ent ◽  
J B Lian ◽  
J L Stein ◽  
G S Stein
Keyword(s):  
Cell Cycle ◽  
Transcriptional Regulation ◽  
Dna Binding ◽  
Consensus Sequence ◽  
Proximal Promoter ◽  
Gene Promoters ◽  
Histone H4 ◽  
Dna Interactions ◽  
Protein Dna Interactions ◽  
Diploid Cells

Transcriptional regulation of vertebrate histone genes during the cell cycle is mediated by several factors interacting with a series of cis-acting elements located in the 5' regions of these genes. The arrangement of these promoter elements is different for each gene. However, most histone H4 gene promoters contain a highly conserved sequence immediately upstream of the TATA box (H4 subtype consensus sequence), and this region in the human H4 gene FO108 is involved in cell cycle control. The sequence-specific interaction of nuclear factor HiNF-D with this key proximal promoter element of the H4-FO108 gene is cell cycle regulated in normal diploid cells (J. Holthuis, T.A. Owen, A.J. van Wijnen, K.L. Wright, A. Ramsey-Ewing, M.B. Kennedy, R. Carter, S.C. Cosenza, K.J. Soprano, J.B. Lian, J.L. Stein, and G.S. Stein, Science, 247:1454-1457, 1990). Here, we show that this region of the H4-FO108 gene represents a composite protein-DNA interaction domain for several distinct sequence-specific DNA-binding activities, including HiNF-D, HiNF-M, and HiNF-P. Factor HiNF-P is similar to H4TF-2, a DNA-binding activity that is not cell cycle regulated and that interacts with the analogous region of the H4 gene H4.A (F. LaBella and N. Heintz, Mol. Cell. Biol. 11:5825-5831, 1991). The H4.A gene fails to interact with factors HiNF-M and HiNF-D owing to two independent sets of specific nucleotide variants, indicating differences in protein-DNA interactions between these H4 genes. Cytosine methylation of a highly conserved CpG dinucleotide interferes with binding of HiNF-P/H4TF-2 to both the H4-FO108 and H4.A promoters, but no effect is observed for either HiNF-M or HiNF-D binding to the H4-FO108 gene. Thus, strong evolutionary conservation of the H4 consensus sequence may be related to combinatorial interactions involving overlapping and interdigitated recognition nucleotides for several proteins, whose activities are regulated independently. Our results also suggest molecular complexity in the transcriptional regulation of distinct human H4 genes.

scholarly journals Overlapping and CpG methylation-sensitive protein-DNA interactions at the histone H4 transcriptional cell cycle domain: distinctions between two human H4 gene promoters

1992 ◽  
Vol 12 (7) ◽  
pp. 3273-3287
Author(s):  
A J van Wijnen ◽  
F M van den Ent ◽  
J B Lian ◽  
J L Stein ◽  
G S Stein
Keyword(s):  
Cell Cycle ◽  
Transcriptional Regulation ◽  
Dna Binding ◽  
Consensus Sequence ◽  
Proximal Promoter ◽  
Gene Promoters ◽  
Histone H4 ◽  
Dna Interactions ◽  
Protein Dna Interactions ◽  
Diploid Cells

Transcriptional regulation of vertebrate histone genes during the cell cycle is mediated by several factors interacting with a series of cis-acting elements located in the 5' regions of these genes. The arrangement of these promoter elements is different for each gene. However, most histone H4 gene promoters contain a highly conserved sequence immediately upstream of the TATA box (H4 subtype consensus sequence), and this region in the human H4 gene FO108 is involved in cell cycle control. The sequence-specific interaction of nuclear factor HiNF-D with this key proximal promoter element of the H4-FO108 gene is cell cycle regulated in normal diploid cells (J. Holthuis, T.A. Owen, A.J. van Wijnen, K.L. Wright, A. Ramsey-Ewing, M.B. Kennedy, R. Carter, S.C. Cosenza, K.J. Soprano, J.B. Lian, J.L. Stein, and G.S. Stein, Science, 247:1454-1457, 1990). Here, we show that this region of the H4-FO108 gene represents a composite protein-DNA interaction domain for several distinct sequence-specific DNA-binding activities, including HiNF-D, HiNF-M, and HiNF-P. Factor HiNF-P is similar to H4TF-2, a DNA-binding activity that is not cell cycle regulated and that interacts with the analogous region of the H4 gene H4.A (F. LaBella and N. Heintz, Mol. Cell. Biol. 11:5825-5831, 1991). The H4.A gene fails to interact with factors HiNF-M and HiNF-D owing to two independent sets of specific nucleotide variants, indicating differences in protein-DNA interactions between these H4 genes. Cytosine methylation of a highly conserved CpG dinucleotide interferes with binding of HiNF-P/H4TF-2 to both the H4-FO108 and H4.A promoters, but no effect is observed for either HiNF-M or HiNF-D binding to the H4-FO108 gene. Thus, strong evolutionary conservation of the H4 consensus sequence may be related to combinatorial interactions involving overlapping and interdigitated recognition nucleotides for several proteins, whose activities are regulated independently. Our results also suggest molecular complexity in the transcriptional regulation of distinct human H4 genes.

Protein-DNA interactions in vivo upstream of a cell cycle-regulated human H4 histone gene

Science ◽  
1987 ◽  
Vol 236 (4806) ◽  
pp. 1308-1311 ◽  
Author(s):  
U Pauli ◽  
S Chrysogelos ◽  
G Stein ◽  
J Stein ◽  
H Nick
Keyword(s):  
Cell Cycle ◽  
Histone Gene ◽  
Dna Interactions ◽  
Protein Dna Interactions ◽  
A Cell

Functional Role for Sp1 in the Transcriptional Amplification of a Cell Cycle Regulated Histone H4 Gene

Biochemistry ◽  
1995 ◽  
Vol 34 (23) ◽  
pp. 7648-7658 ◽  
Author(s):  
Mark J. Birnbaum ◽  
Kenneth L. Wright ◽  
Andre J. van Wijnen ◽  
Anna L. Ramsey-Ewing ◽  
Michael T. Bourke ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Functional Role ◽  
Histone H4 ◽  
A Cell ◽  
Transcriptional Amplification ◽  
Histone H4 Gene

Cell cycle regulation of a mouse histone H4 gene requires the H4 promoter

1987 ◽  
Vol 7 (3) ◽  
pp. 1048-1054
Author(s):  
A Seiler-Tuyns ◽  
B M Paterson
Keyword(s):  
Cell Cycle ◽  
Shuttle Vector ◽  
Constitutive Expression ◽  
Mrna Levels ◽  
Histone H4 ◽  
Coding Region ◽  
Regulated Expression ◽  
Arrest Growth ◽  
Globin Promoter ◽  
Histone H4 Gene

The mouse histone H4 gene, when stably transformed into L cells on the PSV2gpt shuttle vector, is cell cycle regulated in parallel with the endogenous H4 genes. This was determined in exponentially growing pools of transformants fractionated into cell cycle-specific stages by centrifugal elutriation, a method for purifying cells at each stage of the cell cycle without the use of treatments that arrest growth. Linker additions in the 5' noncoding region of the H4 RNA or in the coding region of the gene did not affect the cell cycle-regulated expression of the modified H4 gene even though the overall level of expression was altered. However, replacing the H4 promoter with the human alpha-2 globin promoter, so that the histone transcript produced by the chimeric gene remains essentially unchanged, resulted in the constitutive expression of H4 mRNA during all phases of the cell cycle with no net increase in H4 mRNA levels during the G1-to-S transition. From these results we conclude that all the information necessary for the cell cycle-regulated expression of the H4 gene is contained in the 5.2-kilobase subclone used in these studies with 228 nucleotides of 5'-flanking DNA and that the increase in H4 mRNA during the G1-to-S transition in the cell cycle is mediated by the H4 promoter and not by the increased stability of the H4 RNA.

scholarly journals Identification of HiNF-P, a Key Activator of Cell Cycle-Controlled Histone H4 Genes at the Onset of S Phase

2003 ◽  
Vol 23 (22) ◽  
pp. 8110-8123 ◽  
Author(s):  
Partha Mitra ◽  
Rong-Lin Xie ◽  
Ricardo Medina ◽  
Hayk Hovhannisyan ◽  
S. Kaleem Zaidi ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Progression ◽  
Cyclin E ◽  
S Phase ◽  
Phase Cell ◽  
Regulatory Sequences ◽  
Histone H4 ◽  
Restriction Point ◽  
Histone H4 Gene

ABSTRACT At the G1/S phase cell cycle transition, multiple histone genes are expressed to ensure that newly synthesized DNA is immediately packaged as chromatin. Here we have purified and functionally characterized the critical transcription factor HiNF-P, which is required for E2F-independent activation of the histone H4 multigene family. Using chromatin immunoprecipitation analysis and ligation-mediated PCR-assisted genomic sequencing, we show that HiNF-P interacts with conserved H4 cell cycle regulatory sequences in vivo. Antisense inhibition of HiNF-P reduces endogenous histone H4 gene expression. Furthermore, we find that HiNF-P utilizes NPAT/p220, a substrate of the cyclin E/cyclin-dependent kinase 2 (CDK2) kinase complex, as a key coactivator to enhance histone H4 gene transcription. The biological role of HiNF-P is reflected by impeded cell cycle progression into S phase upon antisense-mediated reduction of HiNF-P levels. Our results establish that HiNF-P is the ultimate link in a linear signaling pathway that is initiated with the growth factor-dependent induction of cyclin E/CDK2 kinase activity at the restriction point and culminates in the activation of histone H4 genes through HiNF-P at the G1/S phase transition.

Sign in / Sign up

Export Citation Format

Share Document