作者: S Harroch , M Revel , J Chebath
DOI: 10.1016/S0021-9258(18)47177-3
关键词: Cell biology 、 Transcription factor 、 Biology 、 Molecular biology 、 Transcription preinitiation complex 、 Consensus sequence 、 STAT1 、 Protein subunit 、 Enhancer RNAs 、 Enhancer 、 Transcription (biology)
摘要: Interferons (IFNs), as well some interleukins, growth factors, and hormones, all induce tyrosine phosphorylation of STAT1 additional transcription factors similar sizes. These are activated to translocate nucleus bind enhancers consensus sequence TTnCnnnAA (gamma-IFN sequence-like enhancers). In mammary cells or hybridoma B9 cells, four distinct tyrosine-phosphorylated complexes by interleukin-6 (IL-6) IFN-beta were observed: pIRFA I, II, III (of increasing electrophoretic mobility). The have unequal affinities for different genes; they with kinetics extents IL-6 IFNs. band isolated from IL-6-stimulated revealed three DNA-interacting components: two large subunits 91 98 kDa, a small component 46 kDa not seen in other analyzed. One the may be APRF/STAT3, since reacted anti-APRF antibodies do I II. However, did react STAT1, indicating is pIRFA. Complex which anti-acute phase response factor also anti-STAT1 antibodies, whereas complex only was resistant N-ethylmaleimide. By its multimeric subunit structure cytokine enhancer specificities, slowly migrating appears novel acting on subset gamma-IFN enhancers.