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

Journal article
Authors Frédéric V Stanger
Björn Marcus Burmann
Alexander Harms
Hugo Aragão
Adam Mazur
Timothy Sharpe
Christoph Dehio
Sebastian Hiller
Tilman Schirmer
Published in Proceedings of the National Academy of Sciences of the United States of America
Volume 113
Issue 5
Pages E529-37
ISSN 1091-6490
Publication year 2016
Published at
Pages E529-37
Language en
Links dx.doi.org/10.1073/pnas.1516930113
www.ncbi.nlm.nih.gov/entrez/query.f...
Keywords Bacterial Proteins, metabolism, Biopolymers, metabolism, Cyclic AMP, metabolism, DNA Gyrase, metabolism, Models, Molecular, Neisseria meningitidis, enzymology, Nucleotidyltransferases, metabolism
Subject categories Structural Biology

Abstract

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 α-helix (αinh) that partly obstructs the active site. For the single-domain class III Fic proteins, the αinh is located at the C terminus and its deletion relieves autoinhibition. 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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Utskriftsdatum: 2019-11-14