Construction of a novel oligonucleotide array‐based transcription factor interaction assay platform and its uses for profiling STAT1 cofactors in mouse fibroblast cells. Issue 16 (22nd July 2013)
- Record Type:
- Journal Article
- Title:
- Construction of a novel oligonucleotide array‐based transcription factor interaction assay platform and its uses for profiling STAT1 cofactors in mouse fibroblast cells. Issue 16 (22nd July 2013)
- Main Title:
- Construction of a novel oligonucleotide array‐based transcription factor interaction assay platform and its uses for profiling STAT1 cofactors in mouse fibroblast cells
- Authors:
- Zeng, Lingqin
Sun, Yimin
Xie, Lan
Wei, Li
Ren, Yonghong
Zhao, Jianqing
Qin, Wenyan
Mitchelson, Keith
Cheng, Jing - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Here, we describe a novel oligonucleotide array‐based transcription factor (TF) interaction assay platform that can directly identify cointeracting TF complexes following binding to their regulatory DNA elements. This platform that combines immuno‐coprecipitation technology with our previously reported oligonucleotide array‐based TF assay (OATFA), is named targeted immuno‐coprecipitation OATFA (TIC‐OATFA). We illustrate use of the system to identify interaction partners of STAT1 (signal transducer and activator of transcription proteins 1) in mouse fibroblasts. Several previously known partners of STAT1, as well as new partners, were identified by TIC‐OATFA, including the upstream stimulatory factors 1 and 2 (USF1, USF2), nuclear factor of activated T cells, TATA box‐binding protein, nuclear factor erythroid‐derived 2, nuclear factor‐kappa B, and nuclear factor 1. Both USF1 and nuclear factor‐kappa B are well known to interact with STAT1, but the other five TFs are previously unreported STAT1 interaction partners. We examined interactions between one new TF, USF2, and STAT1 in detail. USF2 belongs to the group of bHLH‐zip transcription factors, which in a number of diseases including cancers, has enhanced activity. In summary, a novel oligonucleotide array‐based assay platform was developed and used to study interactions between STAT1 and functional TF binding partners, revealing that<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Here, we describe a novel oligonucleotide array‐based transcription factor (TF) interaction assay platform that can directly identify cointeracting TF complexes following binding to their regulatory DNA elements. This platform that combines immuno‐coprecipitation technology with our previously reported oligonucleotide array‐based TF assay (OATFA), is named targeted immuno‐coprecipitation OATFA (TIC‐OATFA). We illustrate use of the system to identify interaction partners of STAT1 (signal transducer and activator of transcription proteins 1) in mouse fibroblasts. Several previously known partners of STAT1, as well as new partners, were identified by TIC‐OATFA, including the upstream stimulatory factors 1 and 2 (USF1, USF2), nuclear factor of activated T cells, TATA box‐binding protein, nuclear factor erythroid‐derived 2, nuclear factor‐kappa B, and nuclear factor 1. Both USF1 and nuclear factor‐kappa B are well known to interact with STAT1, but the other five TFs are previously unreported STAT1 interaction partners. We examined interactions between one new TF, USF2, and STAT1 in detail. USF2 belongs to the group of bHLH‐zip transcription factors, which in a number of diseases including cancers, has enhanced activity. In summary, a novel oligonucleotide array‐based assay platform was developed and used to study interactions between STAT1 and functional TF binding partners, revealing that USF2 and potentially four other new TFs are partners of STAT1 in an IFN‐γ stimulated mouse fibroblast cell line.</p> </abstract> … (more)
- Is Part Of:
- Proteomics. Volume 13:Issue 16(2013:Aug.)
- Journal:
- Proteomics
- Issue:
- Volume 13:Issue 16(2013:Aug.)
- Issue Display:
- Volume 13, Issue 16 (2013)
- Year:
- 2013
- Volume:
- 13
- Issue:
- 16
- Issue Sort Value:
- 2013-0013-0016-0000
- Page Start:
- 2377
- Page End:
- 2385
- Publication Date:
- 2013-07-22
- Subjects:
- Proteins -- Separation -- Periodicals
Bioinformatics -- Periodicals
Proteomics -- Periodicals
Genomes -- Periodicals
Molecular genetics -- Periodicals
572.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1615-9861 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/pmic.201200521 ↗
- Languages:
- English
- ISSNs:
- 1615-9853
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.178000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4368.xml