The PEST-like sequence of I kappa B alpha is responsible for inhibition of DNA binding but not for cytoplasmic retention of c-Rel or RelA homodimers.

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摘要：

In most cells, proteins belonging to the /NF-kappa B family of factors are held in inactive form in the by an , . Stimulation of the cells leads to degradation of the inhibitor and transit of active /NF-kappa B dimers to the . is also able to inhibit by /NF-kappa B dimers in vitro, suggesting that it may perform the same function in cells when the activating signal is no longer present. Structurally, the molecule can be divided into three sections: a 70-amino-acid N terminus with no known function, a 205-residue midsection composed of six ankyrin-like repeats, and a very acidic 42-amino-acid C terminus that resembles a PEST sequence. In this study we examined how the structural elements of the protein correlate with its functional capabilities both in vitro and in vivo. Using a battery of mutants, we show that (i) a dimer binds a single molecule, (ii) the acidic C-terminal region of is not required for protein-and does not mask the nuclear signal of the dimer, (iii) the same C-terminal region is required for inhibition of , and (iv) this inhibition may be accomplished by direct interaction between the PEST-like region and the region of one of the subunits of the dimer.

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关键词：

CALCIUM CARBONATE CRYSTALLIZATION DERMATAN SULFATE PROTEOGLYCAN EGGSHELL ORGANIC MATRIX

DOI：

10.1016/0945-053X(95)90008-X

被引量：

263

年份：

1995