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An atypical aspartic protease modulates lateral root development in Arabidopsis thaliana

ABSTRACT: We determined the specificity profile of recombinant ASPR1 (Atypical Aspartic Protease in Roots 1) using proteome-derived libraries. Although rASPR1 preferred hydrophobic amino acids in the S1 subsite, which is in line with what was previously described for other APs, rASPR1 also displayed a clear preference for accommodating asparagine and lysine in S1, a characteristic only reported so far for fungal APs. Both primary and secondary specificity preferences of rASPR1 thus revealed unique specificity requirements similar to fungal APs that are unprecedented for plant APs.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Suspension Culture, Blood Cell, Monocyte, Blood

SUBMITTER: Sandra Anjo

LAB HEAD: Isaura Simões

PROVIDER: PXD010355 | Pride | 2020-03-19

REPOSITORIES: Pride

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An atypical aspartic protease modulates lateral root development in Arabidopsis thaliana.

Soares André A Niedermaier Stefan S Faro Rosário R Loos Andreas A Manadas Bruno B Faro Carlos C Huesgen Pitter F PF Cheung Alice Y AY Simões Isaura I

Journal of experimental botany 20190401 7

Few atypical aspartic proteases (APs) present in plants have been functionally studied to date despite having been implicated in developmental processes and stress responses. Here we characterize a novel atypical AP that we name Atypical Aspartic Protease in Roots 1 (ASPR1), denoting its expression in Arabidopsis roots. Recombinant ASPR1 produced by transient expression in Nicotiana benthamiana was active and displayed atypical properties, combining optimum acidic pH, partial sensitivity to peps ...[more]

PMID: 30778561

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Project description:Aspergillus fumigatus, a common airborne fungus, has been reported as one of the most frequent agents of human fungal infections. However, A. fumigatus conidia atmospheric resistance and longevity, and their aging mechanism are unknown. Therefore, the main purpose of this work is to clarify the main processes associated with conidial adaptation to nutrient limitation, similar to those found in their atmospheric transport. To that a time course evaluation of the changes in the proteome and in the ultrastructure of A. fumigatus’ conidia subjected to limiting nutrient conditions were performed, allowing a comprehensive characterization of conidia cells behavior and, revealing possible targets for the development of new antifungal medicines and improve infection control strategies. In the proposed work, a total of 712 proteins were identified and compared in the A. fumigatus conidia, with 387 proteins presenting significant differences among the considered conditions. These 387 proteins were then grouped into clusters according to similarities in their dynamic profile (relative levels) among the three points in time analyzed, and four completely distinct profiles can be observed. According with the proteomics changes, it was observed that the conidia go from a highly active metabolic state to a dormant state, and culminate in a cell autolysis state revealed by increased levels of hydrolytic enzymes. The proteomics alterations observed were further corroborate with the structural results, where it was observed changes in mitochondria, nucleus, and plasma membrane ultrastructure, consistent with an apoptotic process. Altogether the results indicate that the changes in protein levels anticipated those in cell morphology, clearly highlighting the need for further studies that may lead to significant improvement in infection control strategies. Additionally, a total of 28 proteins were identified with one acetylated peptide. Among them, it was possible to quantify the acetylation levels in 21 proteins with 11 presenting a statistical meaningful difference between the tested time points. Furthermore, from the proteins evaluated, all except the protein Histone H3, presented N-terminal acetylation. In the case of the Histone H3, the modification was observed at the lysine 56. In general, the proteins regulated by acetylation quantified in our study could be grouped into four distinct groups and although only some of the proteins have a statistical meaningful variation between the experimental time points, those proteins are spread along the different groups. Moreover, statistical variation if observed for all the proteins belonging to the group of proteins that have higher acetylation levels at time 15 minutes. In conclusion, this work presents a comprehensive characterization of the proteomics changes associated with the adaptive mechanism of Aspergillus fumigatus’ conidia to nutrient restriction, raveling some on the main pathways associated with such capacity. Furthermore, this proteomic characterization is associated with the conidia’s ultrastructural evaluation allowing to link the changes observed at the proteome level with the respective phenotype. Finally, it was also presented an evaluation of the levels of the protein acetylation, one of the principal regulatory PTMs in eukaryotes. Therefore, the present study may be an important dataset to be used as a tool to understand and identified potential targets associated with conidia resistance, and therefore improving infection control strategies.

Project description:Rationale: Epicardial adipose tissue (EAT) has been independently associated with non-calcified, high-risk coronary plaques in low-to intermediate risk subjects. Recently, a bidirectional communication was shown between EAT and diseased coronary arteries. In high-risk patients it is unknown whether quantitative measures of EAT can capture, and which molecular players are involved in this mutual interplay. Objective: In a high-risk population, we aimed to determine how the volume of EAT is linked to coronary artery disease (CAD) and to identify potential EAT-deregulated pathways in CAD patients specifically related to coronary artery calcification (CAC). Methods and Results: In a prospective cohort of 574 degenerative severe aortic stenosis patients referred to cardiac surgery, we quantified fat depots by computed tomography (CT) and performed a comparative quantitative proteomics of thoracic fat, including EAT, mediastinal (MAT) and subcutaneous (SAT) adipose tissues. We did not find an independent association of EAT volume with the severity, distribution and complexity of coronary stenosis in invasive coronary angiography. Although, EAT volume was correlated with high CAC, its cardiovascular risk factors-adjusted association was not significant. Taking as reference non-CAD matched-patients and compared to MAT and SAT, EAT proteomic signature of CAD was characterized by up-regulation of pro-calcifying annexins (Annexin A2, ANXA2), fatty acid binding transporters (FABP4) and inflammatory signaling proteins, and by down-regulation of fetuin-A and redox state regulatory enzymes. In EAT, ANXA2 regulation was positively correlated with CAC. EAT gene expression studies confirmed overexpression of ANXA2 and FABP4 in CAD, but no expression of FETUA was detected. Compared with non-CAD, fetuin-A circulating levels were higher in CAD, whereas no fetuin-A pericardial fluid differences were found. Conclusions: In this high-risk cohort, EAT presented an imbalance of pro-calcifying, pro-inflammatory and lipid transporters mediators. These local EAT-mediated regulatory mechanisms were not reflected by the CT volume of EAT alone.

Dataset Information

An atypical aspartic protease modulates lateral root development in Arabidopsis thaliana

Publications

An atypical aspartic protease modulates lateral root development in Arabidopsis thaliana.

Similar Datasets

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