Pip, a novel IRF family member, is a lymphoid-specific, PU.1-dependent transcriptional activator
| Autor: | Ursula Storb, Harinder Singh, Charles F. Eisenbeis |
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| Rok vydání: | 1995 |
| Předmět: |
Molecular Sequence Data
Retroviridae Proteins Oncogenic Biology Cell Line Transcription (biology) Genetics Humans Amino Acid Sequence Lymphocytes Cloning Molecular Enhancer Peptide sequence Gene Ternary complex Regulation of gene expression Base Sequence Molecular biology DNA-Binding Proteins Gene Expression Regulation Interferon Regulatory Factors Trans-Activators Phosphorylation Sequence Alignment Transcription Factors Developmental Biology Interferon regulatory factors |
| Zdroj: | Genes & Development. 9:1377-1387 |
| ISSN: | 1549-5477 0890-9369 |
| DOI: | 10.1101/gad.9.11.1377 |
| Popis: | The immunoglobulin light-chain gene enhancers E kappa 3', E lambda 2-4, and E lambda 3-1 contain a conserved cell type-specific composite element essential for their activities. This element binds a B cell-specific heterodimeric protein complex that consists of the Ets family member PU.1 and a second factor (NF-EM5), whose participation in the formation of the complex is dependent on the presence of DNA-bound PU.1. In this report we describe the cloning and characterization of Pip (PU.1 interaction partner), a lymphoid-specific protein that is most likely NF-EM5. As expected, the Pip protein binds the composite element only in the presence of PU.1; furthermore, the formation of this ternary complex is critically dependent on phosphorylation of PU.1 at serine-148. The Pip gene is expressed specifically in lymphoid tissues in both B- and T-cell lines. When coexpressed in NIH-3T3 cells, Pip and PU.1 function as mutually dependent transcription activators of the composite element. The amino-terminal DNA-binding domain of Pip exhibits a high degree of homology to the DNA-binding domains of members of the interferon regulatory factor (IRF) family, which includes IRF-1, IRF-2, ICSBP, and ISGF3 gamma. |
| Databáze: | OpenAIRE |
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