Sox2 uses multiple domains to associate with proteins present in Sox2-protein complexes

Master regulators, such as Sox2, Oct4 and Nanog, control complex gene networks necessary for the self-renewal and pluripotency of embryonic stem cells (ESC). These master regulators associate with co-activators and co-repressors to precisely control their gene targets. Recent studies using proteomic...

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Bibliographic Details
Published in:PloS one 2010-11, Vol.5 (11), p.e15486-e15486
Main Authors: Cox, Jesse L, Mallanna, Sunil K, Luo, Xu, Rizzino, Angie
Format: Article
Language:English
Subjects:
Analysis
Animals
Binding Sites
Biology
Blotting, Western
Cancer
Cell Line
Cell self-renewal
Deoxyribonucleic acid
DNA
Embryo cells
Embryonic stem cells
Green Fluorescent Proteins - genetics
Green Fluorescent Proteins - metabolism
Growth factors
HDAC2 protein
HEK293 Cells
Histone deacetylase
Histone Deacetylase 1 - metabolism
Histone Deacetylase 2 - metabolism
Humans
Immunoprecipitation
Mass spectrometry
Mice
MicroRNAs
Multiprotein Complexes - metabolism
Nuclear Proteins - metabolism
Oct-4 protein
Pluripotency
Protein Binding
Protein Interaction Mapping - methods
Proteins
Proteomics
Regulators
Repressors
RNA-Binding Proteins - metabolism
Scientific imaging
Self-association
Size distribution
SOXB1 Transcription Factors - genetics
SOXB1 Transcription Factors - metabolism
Stem cells
Studies
Transcription
Transcription (Genetics)
Transcription factors
Transcription Factors - metabolism
Yeast
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Summary:Master regulators, such as Sox2, Oct4 and Nanog, control complex gene networks necessary for the self-renewal and pluripotency of embryonic stem cells (ESC). These master regulators associate with co-activators and co-repressors to precisely control their gene targets. Recent studies using proteomic analysis have identified a large, diverse group of co-activators and co-repressors that associate with master regulators, including Sox2. In this report, we examined the size distribution of nuclear protein complexes containing Sox2 and its associated proteins HDAC1, Sall4 and Lin28. Interestingly, we determined that Sox2 and HDAC1 associate with protein complexes that vary greatly in size; whereas, Lin28 primarily associates with smaller complexes, and Sall4 primarily associates with larger complexes. Additionally, we examined the domains of Sox2 necessary to mediate its association with its partner proteins Sall4, HDAC1 and HDAC2. We determined that Sox2 uses multiple and distinct domains to associate with its partner proteins. We also examined the domains of Sox2 necessary to mediate its self-association, and we determined that Sox2 self-association is mediated through multiple domains. Collectively, these studies provide novel insights into how Sox2 is able to associate with a wide array of nuclear proteins that control gene transcription.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0015486