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B Activity by a Membrane-Transducing Mutant of IB
1
* Bone and Joint Research Unit and
Department of Experimental Pathology, Barts and London School of Medicine and Dentistry, London, United Kingdom
The transcription factor NF-
B is regulated by the IB family
of proteins. The nonphosphorylatable, nondegradable superrepressor
IB
(srIB) mutant is a potent inhibitor of NF-B activity
when expressed in cells. We generated a form of srIB in which its
N terminus is fused to the protein transduction domain of HIV TAT
(TAT-srIB). Purified TAT-srIB protein rapidly and
efficiently entered HeLa or Jurkat T cells. TAT-srIB, when
exogenously added to HeLa cells, inhibited in a dose-dependent manner
TNF-- or IL-1
-induced NF-B activation and binding of NF-B
to its consensus DNA sequence. TAT-srIB was coimmunoprecipitated
with the p65 subunit of NF-B, and this interaction was resistant to
stimulation with IL-1. Therefore, TAT-srIB-mediated inhibition
could result from its nonreversible binding and sequestration of
endogenous NF-B. In contrast, exogenously added TAT-srIB did
not inhibit IL-1-induced activation of extracellular
signal-regulated kinase, c-Jun N-terminal kinase, or p38
mitogen-activated protein kinases or the phosphorylation and
degradation of endogenous IB. These results identify a novel way
for direct regulation of NF-B activity in diverse cell types that
may be useful for therapeutic purposes.
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