A nuclear protein with affinity for the 5' flanking region of a cell cycle dependent human H4 histone gene in vitro

Andre J van Wijnen, J. L. Stein, G. S. Stein

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

A nuclear protein with affinity for the 5' flanking region of a cell cycle dependent human H4 histone gene has been partially purified from nuclear extracts of human HeLa S3 cells. The region involved in the binding of the protein has been localized to an upstream DNA segment using an electrophoretic mobility shift assay. This DNA segment is devoid of RNA polymerase II consensus sequences and contains both homopurinic and A/T rich tracts. Analogous experiments have identified a similar, and perhaps identical, factor that has affinity for a cell cycle dependent human H3 histone gene promoter. This protein appears to bind to a DNA segment containing A/T rich sequences that bear homology with the binding region of the H4 histone promoter. Cell synchronization experiments have shown that the overall affinity of the protein(s) for the H3 and H4 histone 5' flanking regions in vitro is not dramatically altered during the cell cycle. Although the rate of histone gene transcription is modulated during early S phase, transcription occurs throughout the cell cycle. Hence, the protein(s) we have detected here may play a role in the basal expression of these genes.

Original languageEnglish (US)
Pages (from-to)1679-1698
Number of pages20
JournalNucleic Acids Research
Volume15
Issue number4
StatePublished - 1987
Externally publishedYes

Fingerprint

5' Flanking Region
Cell Cycle
Nuclear Proteins
Histones
Affine transformation
Genes
Cells
Gene
Proteins
Protein
DNA
Dependent
Transcription
Promoter
Electrophoretic mobility
RNA
Cell
Assays
Synchronization
RNA Polymerase II

ASJC Scopus subject areas

  • Genetics
  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Health, Toxicology and Mutagenesis
  • Toxicology
  • Genetics(clinical)

Cite this

A nuclear protein with affinity for the 5' flanking region of a cell cycle dependent human H4 histone gene in vitro. / van Wijnen, Andre J; Stein, J. L.; Stein, G. S.

In: Nucleic Acids Research, Vol. 15, No. 4, 1987, p. 1679-1698.

Research output: Contribution to journalArticle

van Wijnen, Andre J ; Stein, J. L. ; Stein, G. S. / A nuclear protein with affinity for the 5' flanking region of a cell cycle dependent human H4 histone gene in vitro. In: Nucleic Acids Research. 1987 ; Vol. 15, No. 4. pp. 1679-1698.
@article{c74826bb36b44404abe781d7b41398a7,
title = "A nuclear protein with affinity for the 5' flanking region of a cell cycle dependent human H4 histone gene in vitro",
abstract = "A nuclear protein with affinity for the 5' flanking region of a cell cycle dependent human H4 histone gene has been partially purified from nuclear extracts of human HeLa S3 cells. The region involved in the binding of the protein has been localized to an upstream DNA segment using an electrophoretic mobility shift assay. This DNA segment is devoid of RNA polymerase II consensus sequences and contains both homopurinic and A/T rich tracts. Analogous experiments have identified a similar, and perhaps identical, factor that has affinity for a cell cycle dependent human H3 histone gene promoter. This protein appears to bind to a DNA segment containing A/T rich sequences that bear homology with the binding region of the H4 histone promoter. Cell synchronization experiments have shown that the overall affinity of the protein(s) for the H3 and H4 histone 5' flanking regions in vitro is not dramatically altered during the cell cycle. Although the rate of histone gene transcription is modulated during early S phase, transcription occurs throughout the cell cycle. Hence, the protein(s) we have detected here may play a role in the basal expression of these genes.",
author = "{van Wijnen}, {Andre J} and Stein, {J. L.} and Stein, {G. S.}",
year = "1987",
language = "English (US)",
volume = "15",
pages = "1679--1698",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "4",

}

TY - JOUR

T1 - A nuclear protein with affinity for the 5' flanking region of a cell cycle dependent human H4 histone gene in vitro

AU - van Wijnen, Andre J

AU - Stein, J. L.

AU - Stein, G. S.

PY - 1987

Y1 - 1987

N2 - A nuclear protein with affinity for the 5' flanking region of a cell cycle dependent human H4 histone gene has been partially purified from nuclear extracts of human HeLa S3 cells. The region involved in the binding of the protein has been localized to an upstream DNA segment using an electrophoretic mobility shift assay. This DNA segment is devoid of RNA polymerase II consensus sequences and contains both homopurinic and A/T rich tracts. Analogous experiments have identified a similar, and perhaps identical, factor that has affinity for a cell cycle dependent human H3 histone gene promoter. This protein appears to bind to a DNA segment containing A/T rich sequences that bear homology with the binding region of the H4 histone promoter. Cell synchronization experiments have shown that the overall affinity of the protein(s) for the H3 and H4 histone 5' flanking regions in vitro is not dramatically altered during the cell cycle. Although the rate of histone gene transcription is modulated during early S phase, transcription occurs throughout the cell cycle. Hence, the protein(s) we have detected here may play a role in the basal expression of these genes.

AB - A nuclear protein with affinity for the 5' flanking region of a cell cycle dependent human H4 histone gene has been partially purified from nuclear extracts of human HeLa S3 cells. The region involved in the binding of the protein has been localized to an upstream DNA segment using an electrophoretic mobility shift assay. This DNA segment is devoid of RNA polymerase II consensus sequences and contains both homopurinic and A/T rich tracts. Analogous experiments have identified a similar, and perhaps identical, factor that has affinity for a cell cycle dependent human H3 histone gene promoter. This protein appears to bind to a DNA segment containing A/T rich sequences that bear homology with the binding region of the H4 histone promoter. Cell synchronization experiments have shown that the overall affinity of the protein(s) for the H3 and H4 histone 5' flanking regions in vitro is not dramatically altered during the cell cycle. Although the rate of histone gene transcription is modulated during early S phase, transcription occurs throughout the cell cycle. Hence, the protein(s) we have detected here may play a role in the basal expression of these genes.

UR - http://www.scopus.com/inward/record.url?scp=0023138224&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023138224&partnerID=8YFLogxK

M3 - Article

C2 - 3029724

AN - SCOPUS:0023138224

VL - 15

SP - 1679

EP - 1698

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 4

ER -