Human H4 histone gene transcription requires the proliferation-specific nuclear factor HiNF-D. Auxiliary roles for HiNF-C (Sp1-like) and HiNF-A (high mobility group-like)

Andre J van Wijnen, K. L. Wright, J. B. Lian, J. L. Stein, G. S. Stein

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

The proximal promoter of the human H4 histone gene F0108 contains two in vivo protein binding domains, sites I and II. In this report we show that these sequences interact with three nuclear factors: HiNF-D, HiNF-C, and HiNF-A. HiNF-C is a metal ion-requiring protein that binds to an Sp1 consensus binding site. HiNF-C and HiNF-A bind independently to the distally located site I, possibly in conjunction with other proteins, and deletion of site I reduces transcription rates 4- to 6-fold in vitro. Factor HiNF-D binds to an H4 histone-specific element (5'-dGGTPyPyTCAATCNGGTCCG, where Py indicates pyrimidine) present in site II that has previously been shown to be essential for in vivo expression of this H4 histone gene. All three binding activities are present in human HeLa S3 cells throughout the cell cycle and in exponentially growing mouse C127 and human HL60 cells. This result is consistent with the transcription of H4 histone genes throughout the cell cycle. However, unlike HiNF-A and HiNFC, HiNF-D is not present in terminally differentiated HL60 cells, in which histone gene transcription is down-regulated. These findings suggest a crucial role for HiNF-D, with an auxiliary role for HiNF-C and possibly HiNF-A, in the regulation of H4 histone gene transcription. Furthermore, the conservation of potential HiNF-D binding sites in mammalian H4 histone gene promoters suggests that HiNF-D has an essential role in the coordinate transcriptional down-regulation of the H4 histone multigene subfamily during the shutdown of proliferation.

Original languageEnglish (US)
Pages (from-to)15034-15042
Number of pages9
JournalJournal of Biological Chemistry
Volume264
Issue number25
StatePublished - 1989
Externally publishedYes

Fingerprint

Transcription
Histones
Genes
HL-60 Cells
Binding Sites
Cells
cdc Genes
Dilatation and Curettage
HeLa Cells
Protein Binding
Metal ions
Conservation
Cell Cycle
Proteins
Down-Regulation
Metals
Ions

ASJC Scopus subject areas

  • Biochemistry

Cite this

Human H4 histone gene transcription requires the proliferation-specific nuclear factor HiNF-D. Auxiliary roles for HiNF-C (Sp1-like) and HiNF-A (high mobility group-like). / van Wijnen, Andre J; Wright, K. L.; Lian, J. B.; Stein, J. L.; Stein, G. S.

In: Journal of Biological Chemistry, Vol. 264, No. 25, 1989, p. 15034-15042.

Research output: Contribution to journalArticle

@article{e84536f2eed54168ab26d896cf147c0d,
title = "Human H4 histone gene transcription requires the proliferation-specific nuclear factor HiNF-D. Auxiliary roles for HiNF-C (Sp1-like) and HiNF-A (high mobility group-like)",
abstract = "The proximal promoter of the human H4 histone gene F0108 contains two in vivo protein binding domains, sites I and II. In this report we show that these sequences interact with three nuclear factors: HiNF-D, HiNF-C, and HiNF-A. HiNF-C is a metal ion-requiring protein that binds to an Sp1 consensus binding site. HiNF-C and HiNF-A bind independently to the distally located site I, possibly in conjunction with other proteins, and deletion of site I reduces transcription rates 4- to 6-fold in vitro. Factor HiNF-D binds to an H4 histone-specific element (5'-dGGTPyPyTCAATCNGGTCCG, where Py indicates pyrimidine) present in site II that has previously been shown to be essential for in vivo expression of this H4 histone gene. All three binding activities are present in human HeLa S3 cells throughout the cell cycle and in exponentially growing mouse C127 and human HL60 cells. This result is consistent with the transcription of H4 histone genes throughout the cell cycle. However, unlike HiNF-A and HiNFC, HiNF-D is not present in terminally differentiated HL60 cells, in which histone gene transcription is down-regulated. These findings suggest a crucial role for HiNF-D, with an auxiliary role for HiNF-C and possibly HiNF-A, in the regulation of H4 histone gene transcription. Furthermore, the conservation of potential HiNF-D binding sites in mammalian H4 histone gene promoters suggests that HiNF-D has an essential role in the coordinate transcriptional down-regulation of the H4 histone multigene subfamily during the shutdown of proliferation.",
author = "{van Wijnen}, {Andre J} and Wright, {K. L.} and Lian, {J. B.} and Stein, {J. L.} and Stein, {G. S.}",
year = "1989",
language = "English (US)",
volume = "264",
pages = "15034--15042",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "25",

}

TY - JOUR

T1 - Human H4 histone gene transcription requires the proliferation-specific nuclear factor HiNF-D. Auxiliary roles for HiNF-C (Sp1-like) and HiNF-A (high mobility group-like)

AU - van Wijnen, Andre J

AU - Wright, K. L.

AU - Lian, J. B.

AU - Stein, J. L.

AU - Stein, G. S.

PY - 1989

Y1 - 1989

N2 - The proximal promoter of the human H4 histone gene F0108 contains two in vivo protein binding domains, sites I and II. In this report we show that these sequences interact with three nuclear factors: HiNF-D, HiNF-C, and HiNF-A. HiNF-C is a metal ion-requiring protein that binds to an Sp1 consensus binding site. HiNF-C and HiNF-A bind independently to the distally located site I, possibly in conjunction with other proteins, and deletion of site I reduces transcription rates 4- to 6-fold in vitro. Factor HiNF-D binds to an H4 histone-specific element (5'-dGGTPyPyTCAATCNGGTCCG, where Py indicates pyrimidine) present in site II that has previously been shown to be essential for in vivo expression of this H4 histone gene. All three binding activities are present in human HeLa S3 cells throughout the cell cycle and in exponentially growing mouse C127 and human HL60 cells. This result is consistent with the transcription of H4 histone genes throughout the cell cycle. However, unlike HiNF-A and HiNFC, HiNF-D is not present in terminally differentiated HL60 cells, in which histone gene transcription is down-regulated. These findings suggest a crucial role for HiNF-D, with an auxiliary role for HiNF-C and possibly HiNF-A, in the regulation of H4 histone gene transcription. Furthermore, the conservation of potential HiNF-D binding sites in mammalian H4 histone gene promoters suggests that HiNF-D has an essential role in the coordinate transcriptional down-regulation of the H4 histone multigene subfamily during the shutdown of proliferation.

AB - The proximal promoter of the human H4 histone gene F0108 contains two in vivo protein binding domains, sites I and II. In this report we show that these sequences interact with three nuclear factors: HiNF-D, HiNF-C, and HiNF-A. HiNF-C is a metal ion-requiring protein that binds to an Sp1 consensus binding site. HiNF-C and HiNF-A bind independently to the distally located site I, possibly in conjunction with other proteins, and deletion of site I reduces transcription rates 4- to 6-fold in vitro. Factor HiNF-D binds to an H4 histone-specific element (5'-dGGTPyPyTCAATCNGGTCCG, where Py indicates pyrimidine) present in site II that has previously been shown to be essential for in vivo expression of this H4 histone gene. All three binding activities are present in human HeLa S3 cells throughout the cell cycle and in exponentially growing mouse C127 and human HL60 cells. This result is consistent with the transcription of H4 histone genes throughout the cell cycle. However, unlike HiNF-A and HiNFC, HiNF-D is not present in terminally differentiated HL60 cells, in which histone gene transcription is down-regulated. These findings suggest a crucial role for HiNF-D, with an auxiliary role for HiNF-C and possibly HiNF-A, in the regulation of H4 histone gene transcription. Furthermore, the conservation of potential HiNF-D binding sites in mammalian H4 histone gene promoters suggests that HiNF-D has an essential role in the coordinate transcriptional down-regulation of the H4 histone multigene subfamily during the shutdown of proliferation.

UR - http://www.scopus.com/inward/record.url?scp=0024431313&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024431313&partnerID=8YFLogxK

M3 - Article

VL - 264

SP - 15034

EP - 15042

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 25

ER -