Proteomic analyses reveal distinct chromatin‐associated and soluble transcription factor complexes. Issue 1 (21st January 2015)
- Record Type:
- Journal Article
- Title:
- Proteomic analyses reveal distinct chromatin‐associated and soluble transcription factor complexes. Issue 1 (21st January 2015)
- Main Title:
- Proteomic analyses reveal distinct chromatin‐associated and soluble transcription factor complexes
- Authors:
- Li, Xu
Wang, Wenqi
Wang, Jiadong
Malovannaya, Anna
Xi, Yuanxin
Li, Wei
Guerra, Rudy
Hawke, David H
Qin, Jun
Chen, Junjie - Abstract:
- Abstract: The current knowledge on how transcription factors (TFs), the ultimate targets and executors of cellular signalling pathways, are regulated by protein–protein interactions remains limited. Here, we performed proteomics analyses of soluble and chromatin‐associated complexes of 56 TFs, including the targets of many signalling pathways involved in development and cancer, and 37 members of the Forkhead box (FOX) TF family. Using tandem affinity purification followed by mass spectrometry (TAP/MS), we performed 214 purifications and identified 2, 156 high‐confident protein–protein interactions. We found that most TFs form very distinct protein complexes on and off chromatin. Using this data set, we categorized the transcription‐related or unrelated regulators for general or specific TFs. Our study offers a valuable resource of protein–protein interaction networks for a large number of TFs and underscores the general principle that TFs form distinct location‐specific protein complexes that are associated with the different regulation and diverse functions of these TFs. Synopsis: Chromatin‐associated and soluble complexes for 56 human transcription factors (TFs), identified by tandem affinity purification followed by mass spectrometry, indicate that distinct binding partners dictate the regulation and functions of TFs. 2, 156 high‐confident interactions are identified by TAP/MS for 56 human TFs, including 37 members of the Forkhead box (FOX) TF family. TFs form distinctAbstract: The current knowledge on how transcription factors (TFs), the ultimate targets and executors of cellular signalling pathways, are regulated by protein–protein interactions remains limited. Here, we performed proteomics analyses of soluble and chromatin‐associated complexes of 56 TFs, including the targets of many signalling pathways involved in development and cancer, and 37 members of the Forkhead box (FOX) TF family. Using tandem affinity purification followed by mass spectrometry (TAP/MS), we performed 214 purifications and identified 2, 156 high‐confident protein–protein interactions. We found that most TFs form very distinct protein complexes on and off chromatin. Using this data set, we categorized the transcription‐related or unrelated regulators for general or specific TFs. Our study offers a valuable resource of protein–protein interaction networks for a large number of TFs and underscores the general principle that TFs form distinct location‐specific protein complexes that are associated with the different regulation and diverse functions of these TFs. Synopsis: Chromatin‐associated and soluble complexes for 56 human transcription factors (TFs), identified by tandem affinity purification followed by mass spectrometry, indicate that distinct binding partners dictate the regulation and functions of TFs. 2, 156 high‐confident interactions are identified by TAP/MS for 56 human TFs, including 37 members of the Forkhead box (FOX) TF family. TFs form distinct complexes on and off chromatin. Different TF‐binding partners dictate the specific regulation and diverse functions of these TFs. Abstract : Chromatin‐associated and soluble complexes for 56 human transcription factors (TFs), identified by tandem affinity purification followed by mass spectrometry, indicate that distinct binding partners dictate the regulation and functions of TFs. … (more)
- Is Part Of:
- Molecular systems biology. Volume 11:Issue 1(2015:Jan.)
- Journal:
- Molecular systems biology
- Issue:
- Volume 11:Issue 1(2015:Jan.)
- Issue Display:
- Volume 11, Issue 1 (2015)
- Year:
- 2015
- Volume:
- 11
- Issue:
- 1
- Issue Sort Value:
- 2015-0011-0001-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2015-01-21
- Subjects:
- forkhead box -- mass spectrometry -- protein–protein interaction -- transcriptional factor
Molecular biology -- Periodicals
Systems biology -- Periodicals
572.8 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1744-4292 ↗
http://www.nature.com/msb/index.html ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.15252/msb.20145504 ↗
- Languages:
- English
- ISSNs:
- 1744-4292
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.856300
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4418.xml