C/EBP-beta drives expression of the nutritionally regulated promoter IA of the acetyl-CoA carboxylase-alpha gene in cattle

Xuanming Shi, Shuzhen Liu, Cornelia C. Metges, Hans Martin Seyfert

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Acetyl-CoA carboxylase-alpha (ACC-α) is the rate-limiting enzyme for de novo fatty acid synthesis. Among the four promoters expressing the bovine gene, promoter IA (PIA) is dominantly active and nutritionally regulated in lipogenic tissues. CCAAT/enhancer binding proteins are crucially involved in regulating the activity of this promoter. We examine here, which member of this family of transcription factors is most important for promoter activation. To differentiate the individual contribution of different members of the C/EBP family transcription factors controlling the ACC-α gene expression in cattle, we established vectors expressing full length (FL) or N-terminally truncated (δN) variants of the C/EBP factors (α, -β, -γ, and -ε) in mammalian cells. Using nuclear extracts of cells expressing the δN-C/EBP factors we determined in electrophoretic mobility shift assays that C/EBPα, -β and -ε, but not C/EBPγ may directly bind to the cognate C/EBP-binding site in the immediate ACC-α PIA. Co-transfection analyses of the various FL-C/EBP expression vectors together with a reporter gene driven by the ACC-α-PIA promoter demonstrated that C/EBPβ has the strongest activation potential. Hence, activity of this factor may be a key regulator of ACC-α-expression in lipogenic tissues.

Original languageEnglish (US)
Pages (from-to)561-567
Number of pages7
JournalBiochimica et Biophysica Acta - Gene Regulatory Mechanisms
Volume1799
Issue number8
DOIs
StatePublished - Aug 1 2010

Fingerprint

CCAAT-Enhancer-Binding Protein-beta
Acetyl-CoA Carboxylase
Genes
Transcription Factors
Chemical activation
Cells
Tissue
CCAAT-Enhancer-Binding Proteins
Electrophoretic mobility
Electrophoretic Mobility Shift Assay
Cell Extracts
Reporter Genes
Gene expression
Transfection
Assays
Fatty Acids
Binding Sites
Drive
Gene Expression
Enzymes

Keywords

  • ACC-alpha
  • C/EBP
  • Cattle
  • Gene expression
  • Isoform
  • Lipid synthesis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics
  • Molecular Biology
  • Structural Biology
  • Medicine(all)

Cite this

C/EBP-beta drives expression of the nutritionally regulated promoter IA of the acetyl-CoA carboxylase-alpha gene in cattle. / Shi, Xuanming; Liu, Shuzhen; Metges, Cornelia C.; Seyfert, Hans Martin.

In: Biochimica et Biophysica Acta - Gene Regulatory Mechanisms, Vol. 1799, No. 8, 01.08.2010, p. 561-567.

Research output: Contribution to journalArticle

@article{c187d46edc1c4cba957c7bec2d700efa,
title = "C/EBP-beta drives expression of the nutritionally regulated promoter IA of the acetyl-CoA carboxylase-alpha gene in cattle",
abstract = "Acetyl-CoA carboxylase-alpha (ACC-α) is the rate-limiting enzyme for de novo fatty acid synthesis. Among the four promoters expressing the bovine gene, promoter IA (PIA) is dominantly active and nutritionally regulated in lipogenic tissues. CCAAT/enhancer binding proteins are crucially involved in regulating the activity of this promoter. We examine here, which member of this family of transcription factors is most important for promoter activation. To differentiate the individual contribution of different members of the C/EBP family transcription factors controlling the ACC-α gene expression in cattle, we established vectors expressing full length (FL) or N-terminally truncated (δN) variants of the C/EBP factors (α, -β, -γ, and -ε) in mammalian cells. Using nuclear extracts of cells expressing the δN-C/EBP factors we determined in electrophoretic mobility shift assays that C/EBPα, -β and -ε, but not C/EBPγ may directly bind to the cognate C/EBP-binding site in the immediate ACC-α PIA. Co-transfection analyses of the various FL-C/EBP expression vectors together with a reporter gene driven by the ACC-α-PIA promoter demonstrated that C/EBPβ has the strongest activation potential. Hence, activity of this factor may be a key regulator of ACC-α-expression in lipogenic tissues.",
keywords = "ACC-alpha, C/EBP, Cattle, Gene expression, Isoform, Lipid synthesis",
author = "Xuanming Shi and Shuzhen Liu and Metges, {Cornelia C.} and Seyfert, {Hans Martin}",
year = "2010",
month = "8",
day = "1",
doi = "10.1016/j.bbagrm.2010.07.002",
language = "English (US)",
volume = "1799",
pages = "561--567",
journal = "Biochimica et Biophysica Acta - Gene Regulatory Mechanisms",
issn = "1874-9399",
publisher = "Elsevier",
number = "8",

}

TY - JOUR

T1 - C/EBP-beta drives expression of the nutritionally regulated promoter IA of the acetyl-CoA carboxylase-alpha gene in cattle

AU - Shi, Xuanming

AU - Liu, Shuzhen

AU - Metges, Cornelia C.

AU - Seyfert, Hans Martin

PY - 2010/8/1

Y1 - 2010/8/1

N2 - Acetyl-CoA carboxylase-alpha (ACC-α) is the rate-limiting enzyme for de novo fatty acid synthesis. Among the four promoters expressing the bovine gene, promoter IA (PIA) is dominantly active and nutritionally regulated in lipogenic tissues. CCAAT/enhancer binding proteins are crucially involved in regulating the activity of this promoter. We examine here, which member of this family of transcription factors is most important for promoter activation. To differentiate the individual contribution of different members of the C/EBP family transcription factors controlling the ACC-α gene expression in cattle, we established vectors expressing full length (FL) or N-terminally truncated (δN) variants of the C/EBP factors (α, -β, -γ, and -ε) in mammalian cells. Using nuclear extracts of cells expressing the δN-C/EBP factors we determined in electrophoretic mobility shift assays that C/EBPα, -β and -ε, but not C/EBPγ may directly bind to the cognate C/EBP-binding site in the immediate ACC-α PIA. Co-transfection analyses of the various FL-C/EBP expression vectors together with a reporter gene driven by the ACC-α-PIA promoter demonstrated that C/EBPβ has the strongest activation potential. Hence, activity of this factor may be a key regulator of ACC-α-expression in lipogenic tissues.

AB - Acetyl-CoA carboxylase-alpha (ACC-α) is the rate-limiting enzyme for de novo fatty acid synthesis. Among the four promoters expressing the bovine gene, promoter IA (PIA) is dominantly active and nutritionally regulated in lipogenic tissues. CCAAT/enhancer binding proteins are crucially involved in regulating the activity of this promoter. We examine here, which member of this family of transcription factors is most important for promoter activation. To differentiate the individual contribution of different members of the C/EBP family transcription factors controlling the ACC-α gene expression in cattle, we established vectors expressing full length (FL) or N-terminally truncated (δN) variants of the C/EBP factors (α, -β, -γ, and -ε) in mammalian cells. Using nuclear extracts of cells expressing the δN-C/EBP factors we determined in electrophoretic mobility shift assays that C/EBPα, -β and -ε, but not C/EBPγ may directly bind to the cognate C/EBP-binding site in the immediate ACC-α PIA. Co-transfection analyses of the various FL-C/EBP expression vectors together with a reporter gene driven by the ACC-α-PIA promoter demonstrated that C/EBPβ has the strongest activation potential. Hence, activity of this factor may be a key regulator of ACC-α-expression in lipogenic tissues.

KW - ACC-alpha

KW - C/EBP

KW - Cattle

KW - Gene expression

KW - Isoform

KW - Lipid synthesis

UR - http://www.scopus.com/inward/record.url?scp=77955653938&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77955653938&partnerID=8YFLogxK

U2 - 10.1016/j.bbagrm.2010.07.002

DO - 10.1016/j.bbagrm.2010.07.002

M3 - Article

C2 - 20637321

AN - SCOPUS:77955653938

VL - 1799

SP - 561

EP - 567

JO - Biochimica et Biophysica Acta - Gene Regulatory Mechanisms

JF - Biochimica et Biophysica Acta - Gene Regulatory Mechanisms

SN - 1874-9399

IS - 8

ER -