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PAS domains in bacterial signal transduction
Erwin C Stuffle1, Mark S Johnson1, Kylie J Watts1
1Division of Microbiology and Molecular Genetics, Alumni Hall for Basic Sciences, Loma Linda University, Loma Linda, CA, 92350, USA.
Current Opinion in Microbiology
|March 1, 2021
Summary
PAS domains are crucial protein structures found across all life. Recent advances reveal new bacterial ligands and expanded functions, enhancing our understanding of cellular signaling mechanisms.
Area of Science:
- Biochemistry and Molecular Biology
- Structural Biology
- Microbiology
Background:
- PAS domains are conserved protein modules present in all kingdoms of life.
- The PAS fold features a conserved cleft for ligand binding, crucial for protein function.
- Recent years have shown a significant increase in identified PAS domain structures and functions.
Purpose of the Study:
- To review recent advancements in understanding PAS domains, particularly in bacteria.
- To highlight newly discovered bacterial PAS ligands and their associated functions.
- To consolidate current knowledge on PAS domain structure-function relationships and signaling mechanisms.
Main Methods:
- Literature review of recent studies on PAS domains.
- Analysis of structural data for PAS domains and their complexes.
- Integration of biochemical and genetic findings related to PAS domain function.
Main Results:
- A substantial increase in the number of identified and structurally resolved PAS domains.
- Discovery of novel ligands that bind to bacterial PAS domains.
- Expansion of the known functional repertoire of bacterial PAS domains, including signal sensing, transduction, and protein interactions.
Conclusions:
- PAS domains are highly versatile signaling modules with diverse roles in bacteria.
- Continued structural and functional studies are crucial for deciphering complex cellular processes regulated by PAS domains.
- The expanding knowledge of PAS domains offers new avenues for understanding and potentially manipulating bacterial signaling pathways.
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