Oligomerization of NTRC at the glnA enhancer is required for transcriptional activation

Susan C. Porter; Anne K. North; Andrew B. Wedel; Sydney Kustu

doi:10.1101/gad.7.11.2258

Oligomerization of NTRC at the glnA enhancer is required for transcriptional activation

Susan C. Porter, Anne K. North, Andrew B. Wedel, Sydney Kustu

Research output: Contribution to journal › Article › peer-review

166 Scopus citations

Abstract

To activate transcription of the glnA gene, the dimeric NTRC protein (nitrogen regulatory protein C) of enteric bacteria binds to an enhancer located ∼100 bp upstream of the promoter. The enhancer is composed of two binding sites for NTRC that are three turns of the DNA helix apart. One role of the enhancer is to tether NTRC in high local concentration near the promoter to allow for its frequent interaction with σ⁵⁴ holoenzyme by DNA looping. We have found that a second role of the enhancer is to ensure oligomerization of NTRC into a complex of at least two dimers that is required for transcriptional activation. Formation of this complex is greatly facilitated by a protein-protein interaction between NTRC dimers that is increased when the protein is phosphorylated.

Original language	English (US)
Pages (from-to)	2258-2273
Number of pages	16
Journal	Genes and Development
Volume	7
Issue number	11
DOIs	https://doi.org/10.1101/gad.7.11.2258
State	Published - 1993
Externally published	Yes

Keywords

Cooperativity
Enhancer
NTRA
NTRC
Oligomerization
Transcriptional regulation

ASJC Scopus subject areas

Genetics
Developmental Biology

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10.1101/gad.7.11.2258

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title = "Oligomerization of NTRC at the glnA enhancer is required for transcriptional activation",

abstract = "To activate transcription of the glnA gene, the dimeric NTRC protein (nitrogen regulatory protein C) of enteric bacteria binds to an enhancer located ∼100 bp upstream of the promoter. The enhancer is composed of two binding sites for NTRC that are three turns of the DNA helix apart. One role of the enhancer is to tether NTRC in high local concentration near the promoter to allow for its frequent interaction with σ54 holoenzyme by DNA looping. We have found that a second role of the enhancer is to ensure oligomerization of NTRC into a complex of at least two dimers that is required for transcriptional activation. Formation of this complex is greatly facilitated by a protein-protein interaction between NTRC dimers that is increased when the protein is phosphorylated.",

keywords = "Cooperativity, Enhancer, NTRA, NTRC, Oligomerization, Transcriptional regulation",

author = "Porter, {Susan C.} and North, {Anne K.} and Wedel, {Andrew B.} and Sydney Kustu",

note = "Funding Information: This work was supported by the Austrian Research Council (project no. 8809). We thank H. Lassmann for stimulating discussions.",

year = "1993",

doi = "10.1101/gad.7.11.2258",

language = "English (US)",

volume = "7",

pages = "2258--2273",

journal = "Genes and Development",

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publisher = "Cold Spring Harbor Laboratory Press",

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TY - JOUR

T1 - Oligomerization of NTRC at the glnA enhancer is required for transcriptional activation

AU - Porter, Susan C.

AU - North, Anne K.

AU - Wedel, Andrew B.

AU - Kustu, Sydney

N1 - Funding Information: This work was supported by the Austrian Research Council (project no. 8809). We thank H. Lassmann for stimulating discussions.

PY - 1993

Y1 - 1993

N2 - To activate transcription of the glnA gene, the dimeric NTRC protein (nitrogen regulatory protein C) of enteric bacteria binds to an enhancer located ∼100 bp upstream of the promoter. The enhancer is composed of two binding sites for NTRC that are three turns of the DNA helix apart. One role of the enhancer is to tether NTRC in high local concentration near the promoter to allow for its frequent interaction with σ54 holoenzyme by DNA looping. We have found that a second role of the enhancer is to ensure oligomerization of NTRC into a complex of at least two dimers that is required for transcriptional activation. Formation of this complex is greatly facilitated by a protein-protein interaction between NTRC dimers that is increased when the protein is phosphorylated.

AB - To activate transcription of the glnA gene, the dimeric NTRC protein (nitrogen regulatory protein C) of enteric bacteria binds to an enhancer located ∼100 bp upstream of the promoter. The enhancer is composed of two binding sites for NTRC that are three turns of the DNA helix apart. One role of the enhancer is to tether NTRC in high local concentration near the promoter to allow for its frequent interaction with σ54 holoenzyme by DNA looping. We have found that a second role of the enhancer is to ensure oligomerization of NTRC into a complex of at least two dimers that is required for transcriptional activation. Formation of this complex is greatly facilitated by a protein-protein interaction between NTRC dimers that is increased when the protein is phosphorylated.

KW - Cooperativity

KW - Enhancer

KW - NTRA

KW - NTRC

KW - Oligomerization

KW - Transcriptional regulation

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SN - 0890-9369

VL - 7

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JO - Genes and Development

JF - Genes and Development

IS - 11

ER -

Oligomerization of NTRC at the glnA enhancer is required for transcriptional activation

Abstract

Keywords

ASJC Scopus subject areas

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