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Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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SP1/2/3 and NfY cooccurency in MEFs

ABSTRACT: Investigation of the binding behaviour of Sp1, Sp2, Sp3 and NF-ya, NF-yb and NF-yc in mouse embryonic fibroblasts and of Sp1, Sp2 and Sp3 in HEK-293 cells reveals distinct binding of the seemingly similar transcription factors Sp1/3 and Sp2.

INSTRUMENT(S): Illumina HiSeq 1000

ORGANISM(S): Mus musculus

SUBMITTER: Bastian Stielow

PROVIDER: E-MTAB-2970 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Zinc finger independent genome-wide binding of Sp2 potentiates recruitment of histone-fold protein Nf-y distinguishing it from Sp1 and Sp3.

Völkel Sara S Stielow Bastian B Finkernagel Florian F Stiewe Thorsten T Nist Andrea A Suske Guntram G

PLoS genetics 20150320 3

Transcription factors are grouped into families based on sequence similarity within functional domains, particularly DNA-binding domains. The Specificity proteins Sp1, Sp2 and Sp3 are paradigmatic of closely related transcription factors. They share amino-terminal glutamine-rich regions and a conserved carboxy-terminal zinc finger domain that can bind to GC rich motifs in vitro. All three Sp proteins are ubiquitously expressed; yet they carry out unique functions in vivo raising the question of ...[more]

PMID: 25793500

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Histone-fold domain protein NF-Y promotes chromatin accessibility for cell type-specific master transcription factors [ChIP-seq]

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2014-08-14 | E-GEOD-56839 | biostudies-arrayexpress

Histone-fold domain protein NF-Y promotes chromatin accessibility for cell type-specific master transcription factors [gene expression]

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