Protein Phosphatase CgPpz1 Regulates Potassium Uptake, Stress Responses and Plant Infection in Colletotrichum gloeosporioides

2021 ◽  
Author(s):  
Yun-Zhao Zhang ◽  
Bing Li ◽  
Yu-Ting Pan ◽  
Yu-Lan Fang ◽  
De-Wei Li ◽  
...  
Keyword(s):  
Stress Responses ◽  
Protein Phosphatase ◽  
Gene Deletion ◽  
Colletotrichum Gloeosporioides ◽  
Asexual Development ◽  
Fungal Development ◽  
Multiple Stress ◽  
Cellular Processes ◽  
Targeted Gene Deletion ◽  
Plant Infection

Protein phosphatases (PPs) play important roles in the regulation of various cellular processes in eukaryotes. The ascomycete Colletotrichum gloeosporioides is a causal agent of anthracnose disease on some important crops and trees. In this study, CgPPZ1, a protein phosphate gene and a homolog of yeast PPZ1, was identified in C. gloeosporioides. Targeted gene deletion showed that CgPpz1 was important for vegetative growth and asexual development, conidial germination, and plant infection. Cytological examinations revealed that CgPpz1 was localized to the cytoplasm. The Cgppz1 mutant was hypersensitive to osmotic stresses, cell wall stressors, and oxidative stressors. Taken together, our results indicated that CgPpz1 plays important role in fungal development and virulence of C. gloeosporioides and multiple stress responses.

scholarly journals Proteomic and Phosphoproteomic Insights into a Signaling Hub Role for Cdc14 in Asexual Development and Multiple Stress Responses in Beauveria bassiana

PLoS ONE ◽  
2016 ◽  
Vol 11 (4) ◽  
pp. e0153007 ◽  
Author(s):  
Zhi-Kang Wang ◽  
Jie Wang ◽  
Jing Liu ◽  
Sheng-Hua Ying ◽  
Xiao-Jun Peng ◽  
...  
Keyword(s):  
Beauveria Bassiana ◽  
Stress Responses ◽  
Asexual Development ◽  
Multiple Stress

scholarly journals Arginine Decarboxylase Is Essential for Pneumococcal Stress Responses

Pathogens ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 286
Author(s):  
Mary Frances Nakamya ◽  
Moses B. Ayoola ◽  
Leslie A. Shack ◽  
Mirghani Mohamed ◽  
Edwin Swiatlo ◽  
...  
Keyword(s):  
Stress Responses ◽  
Critical Role ◽  
Acid Stress ◽  
Arginine Decarboxylase ◽  
Arginine Deiminase ◽  
Dependent Manner ◽  
Cellular Processes ◽  
Opportunistic Human Pathogen ◽  
Thiol Peroxidase ◽  
The Impact

Polyamines such as putrescine, cadaverine, and spermidine are small cationic molecules that play significant roles in cellular processes, including bacterial stress responses and host–pathogen interactions. Streptococcus pneumoniae is an opportunistic human pathogen, which causes several diseases that account for significant morbidity and mortality worldwide. As it transits through different host niches, S. pneumoniae is exposed to and must adapt to different types of stress in the host microenvironment. We earlier reported that S. pneumoniae TIGR4, which harbors an isogenic deletion of an arginine decarboxylase (ΔspeA), an enzyme that catalyzes the synthesis of agmatine in the polyamine synthesis pathway, has a reduced capsule. Here, we report the impact of arginine decarboxylase deletion on pneumococcal stress responses. Our results show that ΔspeA is more susceptible to oxidative, nitrosative, and acid stress compared to the wild-type strain. Gene expression analysis by qRT-PCR indicates that thiol peroxidase, a scavenger of reactive oxygen species and aguA from the arginine deiminase system, could be important for peroxide stress responses in a polyamine-dependent manner. Our results also show that speA is essential for endogenous hydrogen peroxide and glutathione production in S. pneumoniae. Taken together, our findings demonstrate the critical role of arginine decarboxylase in pneumococcal stress responses that could impact adaptation and survival in the host.

scholarly journals Versatile CRISPR/Cas9 Systems for Genome Editing in Ustilago maydis

2021 ◽  
Vol 7 (2) ◽  
pp. 149
Author(s):  
Sarah-Maria Wege ◽  
Katharina Gejer ◽  
Fabienne Becker ◽  
Michael Bölker ◽  
Johannes Freitag ◽  
...  
Keyword(s):  
Genome Editing ◽  
Cell Biology ◽  
Gene Deletion ◽  
Fluorescent Protein ◽  
Point Mutations ◽  
Model Organism ◽  
Ustilago Maydis ◽  
Genomic Locus ◽  
Targeted Gene Deletion ◽  
Molecular Cell Biology

The phytopathogenic smut fungus Ustilago maydis is a versatile model organism to study plant pathology, fungal genetics, and molecular cell biology. Here, we report several strategies to manipulate the genome of U. maydis by the CRISPR/Cas9 technology. These include targeted gene deletion via homologous recombination of short double-stranded oligonucleotides, introduction of point mutations, heterologous complementation at the genomic locus, and endogenous N-terminal tagging with the fluorescent protein mCherry. All applications are independent of a permanent selectable marker and only require transient expression of the endonuclease Cas9hf and sgRNA. The techniques presented here are likely to accelerate research in the U. maydis community but can also act as a template for genome editing in other important fungi.

Targeted gene deletion in Brettanomyces bruxellensis with an expression-free CRISPR-Cas9 system

2020 ◽  
Vol 104 (16) ◽  
pp. 7105-7115
Author(s):  
Cristian Varela ◽  
Caroline Bartel ◽  
Cristobal Onetto ◽  
Anthony Borneman
Keyword(s):  
Gene Deletion ◽  
Brettanomyces Bruxellensis ◽  
Targeted Gene Deletion

scholarly journals W55aEncodes a Novel Protein Kinase That Is Involved in Multiple Stress Responses

2009 ◽  
Vol 51 (1) ◽  
pp. 58-66 ◽  
Author(s):  
Zhao-Shi Xu ◽  
Li Liu ◽  
Zhi-Yong Ni ◽  
Pei Liu ◽  
Ming Chen ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Stress Responses ◽  
Multiple Stress ◽  
Novel Protein

scholarly journals A Chaperone Function of NO CATALASE ACTIVITY1 Is Required to Maintain Catalase Activity and for Multiple Stress Responses in Arabidopsis

2015 ◽  
Vol 27 (3) ◽  
pp. 908-925 ◽  
Author(s):  
Jing Li ◽  
Juntao Liu ◽  
Guoqiang Wang ◽  
Joon-Yung Cha ◽  
Guannan Li ◽  
...  
Keyword(s):  
Stress Responses ◽  
Catalase Activity ◽  
Multiple Stress ◽  
Chaperone Function

Targeted gene deletion of Leishmania major genes encoding developmental stage-specific leishmanolysin (GP63)

1998 ◽  
Vol 27 (3) ◽  
pp. 519-530 ◽  
Author(s):  
Phalgun B. Joshi ◽  
David L. Sacks ◽  
Govind Modi ◽  
W. Robert McMaster
Keyword(s):  
Developmental Stage ◽  
Gene Deletion ◽  
Leishmania Major ◽  
Major Genes ◽  
Targeted Gene Deletion ◽  
Genes Encoding

scholarly journals The split protein phosphatase system

2018 ◽  
Vol 475 (23) ◽  
pp. 3707-3723 ◽  
Author(s):  
Anne Bertolotti
Keyword(s):  
Protein Phosphatase ◽  
Catalytic Subunit ◽  
Regulatory Subunit ◽  
Post Translational Modification ◽  
Antagonistic Action ◽  
Cellular Processes ◽  
Depth Study ◽  
Split Protein ◽  
Phosphatase System ◽  
Physiological Substrates

Reversible phosphorylation of proteins is a post-translational modification that regulates all aspect of life through the antagonistic action of kinases and phosphatases. Protein kinases are well characterized, but protein phosphatases have been relatively neglected. Protein phosphatase 1 (PP1) catalyzes the dephosphorylation of a major fraction of phospho-serines and phospho-threonines in cells and thereby controls a broad range of cellular processes. In this review, I will discuss how phosphatases were discovered, how the view that they were unselective emerged and how recent findings have revealed their exquisite selectivity. Unlike kinases, PP1 phosphatases are obligatory heteromers composed of a catalytic subunit bound to one (or two) non-catalytic subunit(s). Based on an in-depth study of two holophosphatases, I propose the following: selective dephosphorylation depends on the assembly of two components, the catalytic subunit and the non-catalytic subunit, which serves as a high-affinity substrate receptor. Because functional complementation of the two modules is required to produce a selective holophosphatase, one can consider that they are split enzymes. The non-catalytic subunit was often referred to as a regulatory subunit, but it is, in fact, an essential component of the holoenzyme. In this model, a phosphatase and its array of mostly orphan substrate receptors constitute the split protein phosphatase system. The set of potentially generalizable principles outlined in this review may facilitate the study of these poorly understood enzymes and the identification of their physiological substrates.

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