A full-length cDNA encoding a novel type of plant dynamin-like protein, ADL3, was isolated from Arabidopsis thaliana. ADL3 is a high molecular weight GTPase whose GTP-binding domain shows a low homology to those of other plant dynamin-like proteins. ADL3 contains the pleckstrin homology domain as is in mammalian dynamins, although other plant dynamin-like proteins reported lack this domain. The ADL3 gene was expressed weakly in various tissues, except for siliques with high level expression, which is distinct from the case for other plant dynamin-like protein genes. Taken together, it is predicted that the mode of activation of ADL3 is different from those of other plant homologues.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1093/jexbot/51.343.317 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Regulatory Mechanism of Peroxisome Number Reduction Caused by and Deletion in .
J Fungi (Basel)
November 2023
Key Laboratory of Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an 271018, China.
Peroxisomes are single-membrane-bound organelles that play critical roles in eukaryotic cellular functions. Peroxisome quantity is a key factor influencing the homeostasis and pathogenic processes of pathogenic fungi. The aim of the present study was to investigate the underlying mechanisms of the reduction in number of peroxisomes in consequent to and deletion.
View Article and Find Full Text PDFFZL, a dynamin-like protein localized to curved grana edges, is required for efficient photosynthetic electron transfer in .
Front Plant Sci
September 2023
Institute of Plant Science and Resources, Okayama University, Kurashiki, Japan.
Photosynthetic electron transfer and its regulation processes take place on thylakoid membranes, and the thylakoid of vascular plants exhibits particularly intricate structure consisting of stacked grana and flat stroma lamellae. It is known that several membrane remodeling proteins contribute to maintain the thylakoid structure, and one putative example is FUZZY ONION LIKE (FZL). In this study, we re-evaluated the controversial function of FZL in thylakoid membrane remodeling and in photosynthesis.
View Article and Find Full Text PDFConfocal Microscopy Investigations of Biopolymeric PLGA Nanoparticle Uptake in L. Cultured Cells and Plantlet Roots.
Plants (Basel)
June 2023
Department of Environmental Biology, Sapienza University of Rome, P. le Aldo Moro 5, 00185 Rome, Italy.
To date, most endocytosis studies in plant cells have focused on clathrin-dependent endocytosis, while limited evidence is available on clathrin-independent pathways. Since dynamin a is a key protein both in clathrin-mediated endocytosis and in clathrin-independent endocytic processes, this study investigated its role in the uptake of poly-(lactic-co-glycolic) acid (PLGA) nanoparticles (NPs). The experiments were performed on cultured cells and roots of .
View Article and Find Full Text PDFAn expanded arsenal of immune systems that protect bacteria from phages.
Cell Host Microbe
November 2022
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel. Electronic address:
Bacterial anti-phage systems are frequently clustered in microbial genomes, forming defense islands. This property enabled the recent discovery of multiple defense systems based on their genomic co-localization with known systems, but the full arsenal of anti-phage mechanisms remains unknown. We report the discovery of 21 defense systems that protect bacteria from phages, based on computational genomic analyses and phage-infection experiments.
View Article and Find Full Text PDFThe Dynamin-Like GTPase FgSey1 Plays a Critical Role in Fungal Development and Virulence in Fusarium graminearum.
Appl Environ Microbiol
May 2020
Key Laboratory of Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an, China.
, the main pathogenic fungus causing head blight (FHB), produces deoxynivalenol (DON), a key virulence factor, which is synthesized in the endoplasmic reticulum (ER). Sey1/atlastin, a dynamin-like GTPase protein, is known to be required for homotypic fusion of ER membranes, but the functions of this protein are unknown in pathogenic fungi. Here, we characterized Sey1/atlastin homologue FgSey1 in Like Sey1/atlastin, FgSey1 is located in the ER.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!