How 'arm-twisting' by the inducer triggers activation of the MalT transcription factor, a typical signal transduction ATPase with numerous domains (STAND)

Nucleic Acids Research
Olivier Danot

Abstract

Signal transduction ATPases with numerous domains (STAND) get activated through inducer-dependent assembly into multimeric platforms. This switch relies on the conversion of their nucleotide-binding oligomerization domain (NOD) from a closed, ADP-bound form to an open, ATP-bound form. The NOD closed form is stabilized by contacts with the arm, a domain that connects the NOD to the inducer-binding domain called the sensor. How the inducer triggers NOD opening remains unclear. Here, I pinpointed the NOD-arm interface of the MalT STAND transcription factor, and I generated a MalT variant in which this interface can be covalently locked on demand, thereby trapping the NOD in the closed state. By characterizing this locked variant, I found that the inducer is recognized in two steps: it first binds to the sole sensor with low affinity, which then triggers the recruitment of the arm to form a high-affinity arm-sensor inducer-binding site. Strikingly, this high-affinity binding step was incompatible with arm-NOD contacts maintaining the NOD closed. Through this toggling between two mutually exclusive states reminiscent of a single-pole double-throw switch, the arm couples inducer binding to NOD opening, shown here to precede nucleotid...Continue Reading

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Citations

May 22, 2016·Seminars in Cell & Developmental Biology·Octavina C A SukartaAska Goverse
Jul 5, 2019·Journal of Experimental Botany·Jieqiong DengTianzhen Zhang
Feb 26, 2019·Microbial Biotechnology·Grégory BoëlAntoine Danchin
Jun 24, 2017·Annual Review of Phytopathology·Xiaoxiao ZhangMaud Bernoux

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Methods Mentioned

BETA
nucleotide exchange
X-ray
size exclusion chromatography
size-exclusion chromatography
electrophoresis
fluorescence spectroscopy

Software Mentioned

ImageJ
STAND
Modeller
MalT
LRRsearch
HHpred

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