An autoinhibitory mechanism controls RNA‐binding activity of the nitrate‐sensing protein NasR

What is it about?

Although ANTAR domains are widespread in bacterial proteins, it is not known how they recognize RNA, or how signal-responsive domains have evolved to control them. In this study, we identify the most conserved residues of ANTAR domains and examine whether they contribute to RNA-binding activity of Klebsiella oxytoca NasR. We show that when NasR is in its ‘off’ state, residues from its signal-responsive domain sequester key RNA-binding residues as part of an autoinhibitory mechanism. These data provide mechanistic insight into how signaling domains can communicate with RNA-binding output domains.

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