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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America. >Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification
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Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification

机译：Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification

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摘要

Filamentation induced by cyclic AMP (FIC)-domain enzymes catalyze adenylylation or other posttranslational modifications of target proteins to control their function. Recently, we have shown that Fic enzymes are autoinhibited by an alpha-helix (alpha(inh)) that partly obstructs the active site. For the single-domain class III Fic proteins, the ainh is located at the C terminus and its deletion relieves auto-inhibition. However, it has remained unclear how activation occurs naturally. Here, we show by structural, biophysical, and enzymatic analyses combined with in vivo data that the class III Fic protein NmFic from Neisseria meningitidis gets autoadenylylated in cis, thereby autonomously relieving autoinhibition and thus allowing subsequent adenylylation of its target, the DNA gyrase subunit GyrB. Furthermore, we show that NmFic activation is antagonized by tetramerization. The combination of autoadenylylation and tetramerization results in nonmonotonic concentration dependence of NmFic activity and a pronounced lag phase in the progress of target adenylylation. Bioinformatic analyses indicate that this elaborate dual-control mechanism is conserved throughout class III Fic proteins.

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