000114881 001__ 114881
000114881 005__ 20181203021032.0
000114881 0247_ $$2doi$$a10.1074/jbc.M001748200
000114881 037__ $$aARTICLE
000114881 245__ $$aDNA binding specificity of different STAT proteins. Comparison of in vitro specificity with natural target sites
000114881 269__ $$a2001
000114881 260__ $$c2001
000114881 336__ $$aJournal Articles
000114881 500__ $$aSwiss Institute for Experimental Cancer Research (ISREC) 1066 Epalinges, Switzerland. markus.nabholz@isrec.unil.ch
000114881 520__ $$aSTAT transcription factors are expressed in many cell types and bind to similar sequences. However, different STAT gene knock-outs show very distinct phenotypes. To determine whether differences between the binding specificities of STAT proteins account for these effects, we compared the sequences bound by STAT1, STAT5A, STAT5B, and STAT6. One sequence set was selected from random oligonucleotides by recombinant STAT1, STAT5A, or STAT6. For another set including many weak binding sites, we quantified the relative affinities to STAT1, STAT5A, STAT5B, and STAT6. We compared the results to the binding sites in natural STAT target genes identified by others. The experiments confirmed the similar specificity of different STAT proteins. Detailed analysis indicated that STAT5A specificity is more similar to that of STAT6 than that of STAT1, as expected from the evolutionary relationships. The preference of STAT6 for sites in which the half-palindromes (TTC) are separated by four nucleotides (N(4)) was confirmed, but analysis of weak binding sites showed that STAT6 binds fairly well to N(3) sites. As previously reported, STAT1 and STAT5 prefer N(3) sites; however, STAT5A, but not STAT1, weakly binds N(4) sites. None of the STATs bound to half-palindromes. There were no specificity differences between STAT5A and STAT5B.
000114881 700__ $$aEhret, G. B.
000114881 700__ $$aReichenbach, P.
000114881 700__ $$aSchindler, U.
000114881 700__ $$aHorvath, C. M.
000114881 700__ $$aFritz, S.
000114881 700__ $$aNabholz, M.
000114881 700__ $$0244404$$aBucher, P.$$g113607
000114881 773__ $$j276$$k9$$q6675-88$$tJ Biol Chem
000114881 909C0 $$0252244$$pGR-BUCHER$$xU11780
000114881 909CO $$ooai:infoscience.tind.io:114881$$pSV$$particle
000114881 937__ $$aGR-BUCHER-ARTICLE-2001-003
000114881 973__ $$aOTHER$$rREVIEWED$$sPUBLISHED
000114881 980__ $$aARTICLE