scholarly journals Ubiquitin E3 Ligase AaBre1 Responsible for H2B Monoubiquitination Is Involved in Hyphal Growth, Conidiation and Pathogenicity in Alternaria alternata

Genes ◽  
2020 ◽  
Vol 11 (2) ◽  
pp. 229
Author(s):  
Ye Liu ◽  
Jingjing Xin ◽  
Lina Liu ◽  
Aiping Song ◽  
Yuan Liao ◽  
...  
Keyword(s):  
Alternaria Alternata ◽  
E3 Ligase ◽  
Enrichment Analysis ◽  
Hyphal Growth ◽  
Cell Wall Degrading Enzymes ◽  
Ubiquitin E3 Ligase ◽  
Histone 3 ◽  
Go Enrichment ◽  
Genes Encoding ◽  
Conidial Formation

Ubiquitination is one of several post-transcriptional modifications of histone 2B (H2B) which affect the chromatin structure and, hence, influence gene transcription. This study focuses on Alternaria alternata, a fungal pathogen responsible for leaf spot in many plant species. The experiments show that the product of AaBRE1, a gene which encodes H2B monoubiquitination E3 ligase, regulates hyphal growth, conidial formation and pathogenicity. Knockout of AaBRE1 by the homologous recombination strategy leads to the loss of H2B monoubiquitination (H2Bub1), as well as a remarkable decrease in the enrichment of trimethylated lysine 4 on histone 3 (H3K4me3). RNA sequencing assays elucidated that the transcription of genes encoding certain C2H2 zinc-finger family transcription factors, cell wall-degrading enzymes and chitin-binding proteins was suppressed in the AaBRE1 knockout cells. GO enrichment analysis showed that these proteins encoded by the set of genes differentially transcribed between the deletion mutant and wild type were enriched in the functional categories “macramolecular complex”, “cellular metabolic process”, etc. A major conclusion was that the AaBRE1 product, through its effect on histone 2B monoubiquitination and histone 3 lysine 4 trimethylation, makes an important contribution to the fungus’s hyphal growth, conidial formation and pathogenicity.

scholarly journals Comparative analysis of microRNA profiles between wild and cultured Haemaphysalis longicornis (Acari, Ixodidae) ticks

Parasite ◽  
2019 ◽  
Vol 26 ◽  
pp. 18 ◽  
Author(s):  
Jin Luo ◽  
Qiaoyun Ren ◽  
Ze Chen ◽  
Wenge Liu ◽  
Zhiqiang Qu ◽  
...  
Keyword(s):  
Target Genes ◽  
Enrichment Analysis ◽  
Haemaphysalis Longicornis ◽  
Mirna Regulation ◽  
Illumina Hiseq ◽  
Immune Genes ◽  
Host Interaction ◽  
Go Enrichment ◽  
Genes Encoding ◽  
Stressful Stimulation

The miRNA profiles of a Haemaphysalis longicornis wild-type (HLWS) and of a Haemaphysalis longicornis cultured population (HLCS) were sequenced using the Illumina Hiseq 4000 platform combined with bioinformatics analysis and real-time polymerase chain reaction (RT-PCR). A total of 15.63 and 15.48 million raw reads were acquired for HLWS and HLCS, respectively. The data identified 1517 and 1327 known conserved miRNAs, respectively, of which 342 were differentially expressed between the two libraries. Thirty-six novel candidate miRNAs were predicted. To explain the functions of these novel miRNAs, Gene Ontology (GO) analysis was performed. Target gene function prediction identified a significant set of genes related to salivary gland development, pathogen-host interaction and regulation of the defence response to pathogens expressed by wild H. longicornis ticks. Cellular component biogenesis, the immune system process, and responses to stimuli were represented at high percentages in the two tick libraries. GO enrichment analysis showed that the percentages of most predicted functions of the target genes of miRNA were similar, as were certain specific categories of functional enhancements, and that these genes had different numbers and specific functions (e.g., auxiliary transport protein and electron carrier functions). This study provides novel findings showing that miRNA regulation affects the expression of immune genes, indicating a considerable influence of environment-induced stressful stimulation on immune homeostasis. Differences in the living environments of ticks can lead to differences in miRNAs between ticks and provide a basis and a convenient means to screen for genes encoding immune factors in ticks.

Microscopy studies of powdery mildew on summer squash

1991 ◽  
Vol 49 ◽  
pp. 520-521
Author(s):  
John S. Gardner ◽  
W. M. Hess
Keyword(s):  
Powdery Mildew ◽  
Tip Growth ◽  
Hyphal Growth ◽  
Plant Tissues ◽  
Vegetative Hypha ◽  
Powdery Mildews ◽  
Summer Squash ◽  
Conidial Formation ◽  
Polar Tip Growth ◽  
Short Conidiophore

Powdery mildews are characterized by the appearance of spots or patches of a white to grayish, powdery, mildewy growth on plant tissues, entire leaves or other organs. Ervsiphe cichoracearum, the powdery mildew of cucurbits is among the most serious parasites, and the most common. The conidia are formed similar to the process described for Ervsiphe graminis by Cole and Samson. Theconidial chains mature basipetally from a short, conidiophore mother-cell at the base of the fertile hypha which arises holoblastically from the conidiophore. During early development it probably elongates by polar-tip growth like a vegetative hypha. A septum forms just above the conidiophore apex. Additional septa develop in acropetal succession. However, the conidia of E. cichoracearum are more doliform than condia from E. graminis. The purpose of these investigations was to use scanning electron microscopy (SEM) to demonstrate the nature of hyphal growth and conidial formation of E. cichoracearum on field-grown squash leaves.

scholarly journals Regulation of DNA Replication Licensing and Re-Replication by Cdt1

2021 ◽  
Vol 22 (10) ◽  
pp. 5195
Author(s):  
Hui Zhang
Keyword(s):  
Cell Cycle ◽  
Dna Damage ◽  
Dna Replication ◽  
Genome Stability ◽  
E3 Ligase ◽  
S Phase ◽  
Replication Initiation ◽  
Nuclear Antigen ◽  
Repair Synthesis ◽  
Ubiquitin E3 Ligase

In eukaryotic cells, DNA replication licensing is precisely regulated to ensure that the initiation of genomic DNA replication in S phase occurs once and only once for each mitotic cell division. A key regulatory mechanism by which DNA re-replication is suppressed is the S phase-dependent proteolysis of Cdt1, an essential replication protein for licensing DNA replication origins by loading the Mcm2-7 replication helicase for DNA duplication in S phase. Cdt1 degradation is mediated by CRL4Cdt2 ubiquitin E3 ligase, which further requires Cdt1 binding to proliferating cell nuclear antigen (PCNA) through a PIP box domain in Cdt1 during DNA synthesis. Recent studies found that Cdt2, the specific subunit of CRL4Cdt2 ubiquitin E3 ligase that targets Cdt1 for degradation, also contains an evolutionarily conserved PIP box-like domain that mediates the interaction with PCNA. These findings suggest that the initiation and elongation of DNA replication or DNA damage-induced repair synthesis provide a novel mechanism by which Cdt1 and CRL4Cdt2 are both recruited onto the trimeric PCNA clamp encircling the replicating DNA strands to promote the interaction between Cdt1 and CRL4Cdt2. The proximity of PCNA-bound Cdt1 to CRL4Cdt2 facilitates the destruction of Cdt1 in response to DNA damage or after DNA replication initiation to prevent DNA re-replication in the cell cycle. CRL4Cdt2 ubiquitin E3 ligase may also regulate the degradation of other PIP box-containing proteins, such as CDK inhibitor p21 and histone methylase Set8, to regulate DNA replication licensing, cell cycle progression, DNA repair, and genome stability by directly interacting with PCNA during DNA replication and repair synthesis.

The linear ubiquitin E3 ligase-Relish pathway is involved in the regulation of proteostasis in Drosophila muscle during aging

2021 ◽  
Vol 550 ◽  
pp. 184-190
Author(s):  
Banseok Lee ◽  
Changmin Shin ◽  
Myeongcheol Shin ◽  
Byoungyun Choi ◽  
Chunyu Yuan ◽  
...  
Keyword(s):  
E3 Ligase ◽  
Ubiquitin E3 Ligase

scholarly journals High-CO2 Treatment Prolongs the Postharvest Shelf Life of Strawberry Fruits by Reducing Decay and Cell Wall Degradation

Foods ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1649
Author(s):  
Hyang-Lan Eum ◽  
Seung-Hyun Han ◽  
Eun-Jin Lee
Keyword(s):  
Cell Wall ◽  
Shelf Life ◽  
Physiological Mechanism ◽  
Pectate Lyase ◽  
Pectin Methylesterase ◽  
Cell Wall Degradation ◽  
Cell Wall Degrading Enzymes ◽  
High Co2 ◽  
Genes Encoding ◽  
Co2 Treatment

Improved methods are needed to extend the shelf life of strawberry fruits. The objective of this study was to determine the postharvest physiological mechanism of high-CO2 treatment in strawberries. Harvested strawberries were stored at 10 °C after 3 h of exposure to a treatment with 30% CO2 or air. Pectin and gene expression levels related to cell wall degradation were measured to assess the high-CO2 effects on the cell wall and lipid metabolism. Strawberries subjected to high-CO2 treatment presented higher pectin content and firmness and lower decay than those of control fruits. Genes encoding cell wall-degrading enzymes (pectin methylesterase, polygalacturonase, and pectate lyase) were downregulated after high-CO2 treatment. High-CO2 induced the expression of oligogalacturonides, thereby conferring defense against Botrytis cinerea in strawberry fruits, and lowering the decay incidence at seven days after its inoculation. Our findings suggest that high-CO2 treatment can maintain strawberry quality by reducing decay and cell wall degradation.

scholarly journals KCTD proteins as Cullin3 E3 Ligase adapters

2014 ◽  
Vol 70 (a1) ◽  
pp. C305-C305
Author(s):  
Alan Ji ◽  
Gilbert Privé
Keyword(s):  
Crystal Structure ◽  
Structural Characterization ◽  
Dissociation Constants ◽  
E3 Ligase ◽  
Terminal Region ◽  
Btb Domain ◽  
Substrate Protein ◽  
Ubiquitin E3 Ligase ◽  
Ubiquitin Moiety

Cullin3 (Cul3) is an ubiquitin E3 ligase responsible for catalyzing the transfer of an ubiquitin moiety from an E2 enzyme to a target substrate protein. The C-terminal region of Cul3 binds RBX1/E2-ubiquitin, while, the N-terminal region interacts with various BTB domain proteins which serve as substrate adaptors. Previously, our group determined the crystal structures of the homodimeric BTB proteins SPOP and KLHL3 in complex with the N-terminal domain of Cul3, revealing the determinants responsible for the BTB/Cul3 interaction [1, 2]. A second class of BTB-domain containing proteins, the KCTD proteins, are also Cul3 substrate adaptors but these do not share many of the previously determined features for Cul3 binding. Furthermore, KCTD proteins form homotetramers and homopentamers via BTB oligomerization rather than the previously described homodimers. Despite these differences, many KCTD proteins interact with Cul3 with dissociation constants of approximately 50 nM. While the target substrates for many of the KCTD/Cul3 E3 ligase complexes are unknown, recent studies have implicated the GABAβ2 receptor as an interactor of KCTD 8, 12, 12b and 16. Here, we report the pentameric crystal structure of the KCTD9 BTB domain and our progress on the structural characterization of Cul3/KCTD/substrate complexes.

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