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Structures, functions, and regulatory networks of universal stress proteins in clinically relevant pathogenic Bacteria.
- Source :
-
Cellular Signalling . Apr2024, Vol. 116, pN.PAG-N.PAG. 1p. - Publication Year :
- 2024
-
Abstract
- Universal stress proteins are a class of proteins widely present in bacteria, archaea, plants, and invertebrates, playing essential roles in bacterial adaptation to various environmental stresses. The functions of bacterial universal stress proteins are versatile, including resistance to oxidative stress, maintenance of cell wall integrity, DNA damage repair, regulation of cell division and growth, among others. When facing stresses such as temperature changes, pH shifts, fluctuations in oxygen concentration, and exposure to toxins, these proteins can bind to specific DNA sequences and rapidly adjust bacterial metabolic pathways and gene expression patterns to adapt to the new environment. In summary, bacterial universal stress proteins play a crucial role in bacterial adaptability and survival. A comprehensive understanding of bacterial stress response mechanisms and the development of new antibacterial strategies are of great significance. This review summarizes the research progress on the structure, function, and regulatory factors of universal stress proteins in clinically relevant bacteria, aiming to facilitate deeper investigations by clinicians and researchers into universal stress proteins. • Universal stress proteins are crucial for bacterial adaptation to various environmental stresses. • These proteins have versatile functions, including oxidative stress resistance and DNA damage repair. • Understanding bacterial stress response mechanisms is significant for developing new antibacterial strategies. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 08986568
- Volume :
- 116
- Database :
- Academic Search Index
- Journal :
- Cellular Signalling
- Publication Type :
- Academic Journal
- Accession number :
- 175697952
- Full Text :
- https://doi.org/10.1016/j.cellsig.2023.111032