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Interface switch mediates signal transmission in a two-component system.

Mingxing Wang¹, Qiong Guo¹, Kongfu Zhu¹

¹Ministry of Education Key Laboratory for Membraneless Organelles & Cellular Dynamics, Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, 230027 Hefei, P.R. China.

Proceedings of the National Academy of Sciences of the United States of America

|November 17, 2020

Summary

This summary is machine-generated.

This study reveals how the HptRSA two-component system (TCS) in Staphylococcus aureus senses glucose-6-phosphate (G6P) by structural changes in HptA, triggering downstream signaling for bacterial growth.

Keywords:

G6P sensing HptRSA cross-membrane signaling two-component system

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Area of Science:

Microbiology
Molecular Biology
Structural Biology

Background:

Two-component systems (TCS) are crucial for prokaryotic signal transduction.
HptRSA is a TCS involved in glucose-6-phosphate (G6P) uptake and Staphylococcus aureus pathogenesis.
The mechanism of G6P perception and signaling by HptRSA was previously unknown.

Purpose of the Study:

To elucidate the structural mechanism of G6P sensing by the HptRSA two-component system.
To understand how G6P binding to HptA initiates downstream signaling through HptS.
To provide mechanistic insights into bacterial nutrient sensing and TCS activation.

Main Methods:

X-ray crystallography to determine structures of HptA (apo and G6P-bound) and HptA-HptS complexes.
Biochemical assays and mutant analyses of HptA and HptS.
Bacterial growth assays to assess the functional impact of mutations.

Main Results:

G6P binding induces a conformational change in HptA, closing the cleft between its domains.
HptA interacts with the HptS periplasmic domain (HptSp) via distinct interfaces in its G6P-free and G6P-bound states.
G6P binding to HptA switches the interaction interface with HptSp, leading to HptSp conformational changes and downstream signaling initiation.

Conclusions:

A novel mechanism of interface switch-mediated signal transduction by HptRSA has been proposed.
Structural insights into G6P perception and activation of TCS in Staphylococcus aureus.
Expanded understanding of bacterial nutrient sensing and TCS signaling pathways.