Universal stress protein in Malus sieversii confers enhanced drought tolerance

2019 ◽  
Vol 132 (6) ◽  
pp. 825-837
Author(s):  
Meiling Yang ◽  
Shiyou Che ◽  
Yunxiu Zhang ◽  
Hongbin Wang ◽  
Tao Wei ◽  
...  
Keyword(s):  
Drought Tolerance ◽  
Stress Protein ◽  
Universal Stress Protein ◽  
Malus Sieversii

scholarly journals SpUSP, an annexin-interacting universal stress protein, enhances drought tolerance in tomato

2012 ◽  
Vol 63 (15) ◽  
pp. 5593-5606 ◽  
Author(s):  
Rachid Loukehaich ◽  
Taotao Wang ◽  
Bo Ouyang ◽  
Khurram Ziaf ◽  
Hanxia Li ◽  
...  
Keyword(s):  
Drought Tolerance ◽  
Stress Protein ◽  
Universal Stress Protein

The bacterial universal stress protein: function and regulation

2003 ◽  
Vol 6 (2) ◽  
pp. 140-145 ◽  
Author(s):  
Kristian Kvint ◽  
Laurence Nachin ◽  
Alfredo Diez ◽  
Thomas Nyström
Keyword(s):  
Protein Function ◽  
Stress Protein ◽  
Universal Stress Protein

scholarly journals Universal stress protein Rv2624c alters abundance of arginine and enhances intracellular survival by ATP binding in mycobacteria

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Qiong Jia ◽  
Xinling Hu ◽  
Dawei Shi ◽  
Yan Zhang ◽  
Meihao Sun ◽  
...  
Keyword(s):  
Mycobacterium Smegmatis ◽  
Metabolic Pathways ◽  
Biochemical Analysis ◽  
Stress Proteins ◽  
Stress Protein ◽  
Human Monocyte ◽  
Dependent Manner ◽  
Proline Metabolism ◽  
Universal Stress Protein ◽  
Induced Proteins

Abstract The universal stress protein family is a family of stress-induced proteins. Universal stress proteins affect latency and antibiotic resistance in mycobacteria. Here, we showed that Mycobacterium smegmatis overexpressing M. tuberculosis universal stress protein Rv2624c exhibits increased survival in human monocyte THP-1 cells. Transcriptome analysis suggested that Rv2624c affects histidine metabolism, and arginine and proline metabolism. LC-MS/MS analysis showed that Rv2624c affects the abundance of arginine, a modulator of both mycobacteria and infected THP-1 cells. Biochemical analysis showed that Rv2624c is a nucleotide-binding universal stress protein, and an Rv2624c mutant incapable of binding ATP abrogated the growth advantage in THP-1 cells. Rv2624c may therefore modulate metabolic pathways in an ATP-dependent manner, changing the abundance of arginine and thus increasing survival in THP-1 cells.

scholarly journals Inactivation of PadR, the Repressor of the Phenolic Acid Stress Response, by Molecular Interaction with Usp1, a Universal Stress Protein from Lactobacillus plantarum, in Escherichia coli

2009 ◽  
Vol 75 (16) ◽  
pp. 5273-5283 ◽  
Author(s):  
Jérôme Gury ◽  
Hélène Seraut ◽  
Ngoc Phuong Tran ◽  
Lise Barthelmebs ◽  
Stéphanie Weidmann ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Stress Response ◽  
Lactobacillus Plantarum ◽  
Phenolic Acid ◽  
Stress Protein ◽  
Acid Stress ◽  
Universal Stress Protein ◽  
E Coli ◽  
Gram Positive Bacteria ◽  
Acid Stress Response

ABSTRACT The phenolic acid decarboxylase gene padA is involved in the phenolic acid stress response (PASR) in gram-positive bacteria. In Lactobacillus plantarum, the padR gene encodes the negative transcriptional regulator of padA and is cotranscribed with a downstream gene, usp1, which encodes a putative universal stress protein (USP), Usp1, of unknown function. The usp1 gene is overexpressed during the PASR. However, the role and the mechanism of action of the USPs are unknown in gram-positive bacteria. Therefore, to gain insights into the role of USPs in the PASR; (i) a usp1 deletion mutant was constructed; (ii) the two genes padR and usp1 were coexpressed with padA under its own promoter as a reporter gene in Escherichia coli; and (iii) molecular in vitro interactions between the PadR, Usp1, and the padA promoter were studied. Although the usp1 mutant strain retained phenolic acid-dependent PAD activity, it displayed a greater sensitivity to strong acidic conditions compared to that of the wild-type strain. PadR cannot be inactivated directly by phenolic acid in E. coli recombinant cultures but is inactivated by Usp1 when the two proteins are coexpressed in E. coli. The PadR inactivation observed in recombinant E. coli cells was supported by electrophoretic mobility shift assays. Although Usp1 seems not to be absolutely required for the PASR, its capacity to inactivate PadR indicates that it could serve as an important mediator in acid stress response mechanisms through its capacity to interact with transcriptional regulators.

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