Abstract:
:Latent and activated forms of Stat1 and Stat6 have been expressed and purified, enabling biochemical experiments relating to their functional activities. Stat1 bound to a phosphotyrosine peptide derived from the IFN gamma receptor with a KD of 50 nM, whereas Stat6 bound to an IL-4 receptor peptide with a KD of 300 nM. Stat-receptor peptide interactions were specific and dependent upon tyrosine phosphorylation. Activated forms of Stat1 and Stat6 were used to select their optimal DNA binding sites. Stat1 selected a recognition site having dyad half-sites separated by 3 bp. Stat6 selected a recognition site composed of the same dyad half-sites, yet separated by 4 bp. Chimeric Stat1-Stat6 recombinants were expressed, purified, and assayed for receptor coupling and DNA binding specificity. Such studies led to the identification of polypeptide domains that specify these activities. These observations provide a framework for understanding how different cytokines elicit distinctive patterns of gene expression.
journal_name
Immunityjournal_title
Immunityauthors
Schindler U,Wu P,Rothe M,Brasseur M,McKnight SLdoi
10.1016/1074-7613(95)90013-6subject
Has Abstractpub_date
1995-06-01 00:00:00pages
689-97issue
6eissn
1074-7613issn
1097-4180pii
1074-7613(95)90013-6journal_volume
2pub_type
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