Tissue-specific organelle DNA degradation mediated by DPD1 exonuclease

Tang, Lay Yin; Sakamoto, Wataru

doi:10.4161/psb.6.9.16595

Cited by 19 publications

(12 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…, 2007). In support of this, DPD1 expression appears to be up‐regulated during leaf senescence (Tang and Sakamoto, 2011). The other possibility is that ODD in pollen secures the maternal transmission of mtDNAs, although this possibility has not been experimentally confirmed (Matsushima et al.…”

Section: Discussionmentioning

confidence: 79%

Mutations defective in ribonucleotide reductase activity interfere with pollen plastid DNA degradation mediated by DPD1 exonuclease

2012

Self Cite

View full text Add to dashboard Cite

SUMMARYOrganellar DNAs in mitochondria and plastids are present in multiple copies and make up a substantial proportion of total cellular DNA despite their limited genetic capacity. We recently demonstrated that organellar DNA degradation occurs during pollen maturation, mediated by the Mg 2+ -dependent organelle exonuclease DPD1. To further understand organellar DNA degradation, we characterized a distinct mutant (dpd2). In contrast to the dpd1 mutant, which retains both plastid and mitochondrial DNAs, dpd2 showed specific accumulation of plastid DNAs. Multiple abnormalities in vegetative and reproductive tissues of dpd2 were also detected. DPD2 encodes the large subunit of ribonucleotide reductase, an enzyme that functions at the rate-limiting step of de novo nucleotide biosynthesis. We demonstrated that the defects in ribonucleotide reductase indirectly compromise the activity of DPD1 nuclease in plastids, thus supporting a different regulation of organellar DNA degradation in pollen. Several lines of evidence provided here reinforce our previous conclusion that the DPD1 exonuclease plays a central role in organellar DNA degradation, functioning in DNA salvage rather than maternal inheritance during pollen development.

show abstract

Section: Discussionmentioning

confidence: 79%

Mutations defective in ribonucleotide reductase activity interfere with pollen plastid DNA degradation mediated by DPD1 exonuclease

2012

Self Cite

View full text Add to dashboard Cite

show abstract

“…Another marker, S1_299186321 on chromosome 1, is linked to 3'-5' exonuclease. It has been reported that Exonuclease transcripts accumulate at high levels in senescing leaves when stress is applied (Tang and Sakamoto, 2011 ). In addition, a programmed cell death protein (PCD) was found to be linked to markers S1_305729693 and S1_305729831.…”

Section: Discussionmentioning

confidence: 99%

Genome-Wide Association Mapping of Loci Associated with Plant Growth and Forage Production under Salt Stress in Alfalfa (Medicago sativa L.)

Liu

2017

Front. Plant Sci.

View full text Add to dashboard Cite

Salinity tolerance is highly desirable to sustain alfalfa production in marginal lands that have been rendered saline. In this study, we used a diverse panel of 198 alfalfa accessions for mapping loci associated with plant growth and forage production under salt stress using genome-wide association studies (GWAS). The plants were genotyped using genotyping-by-sequencing (GBS). A greenhouse procedure was used for phenotyping four agronomic and physiological traits affected by salt stress, including dry weight (DW), plant height (PH), leaf chlorophyll content (LCC), and stomatal conductance (SC). For each trait, a stress susceptibility index (SSI) was used to evaluate plant performance under stressed and non-stressed conditions. Marker-trait association identified a total of 42 markers significantly associated with salt tolerance. They were located on all chromosomes except chromosome 2 based on the alignment of their flanking sequences to the reference genome (Medicago truncatula). Of those identified, 13 were associated with multiple traits. Several loci identified in the present study were also identified in previous reports. BLAST search revealed that 19 putative candidate genes linked to 24 significant markers. Among them, B3 DNA-binding protein, Thiaminepyrophosphokinase and IQ calmodulin-binding motif protein were identified among multiple traits in the present and previous studies. With further investigation, these markers and candidates would be useful for developing markers for marker-assisted selection in breeding programs to improve alfalfa cultivars with enhanced tolerance to salt stress.

show abstract

“…It seems that the most remarkable feature of both CAN nucleases is their unusual cellular localization. Nucleases that have been studied so far were identified in cellular compartments containing nucleic acids, such as the nucleus [ 1 ], plastids and mitochondria [ 34 ] or in the organelles where they are stored before final application, for example, vacuole [ 12 ], lysosome [ 1 ] and other intracellular membrane vesicles [ 6 ]. To our knowledge, the CAN enzymes described in this paper are the only eukaryotic nucleases associated with the plasma membrane.…”

Section: Discussionmentioning

confidence: 99%

Plant plasma membrane-bound staphylococcal-like DNases as a novel class of eukaryotic nucleases

et al. 2012

View full text Add to dashboard Cite

BackgroundThe activity of degradative nucleases responsible for genomic DNA digestion has been observed in all kingdoms of life. It is believed that the main function of DNA degradation occurring during plant programmed cell death is redistribution of nucleic acid derived products such as nitrogen, phosphorus and nucleotide bases. Plant degradative nucleases that have been studied so far belong mainly to the S1-type family and were identified in cellular compartments containing nucleic acids or in the organelles where they are stored before final application. However, the explanation of how degraded DNA components are exported from the dying cells for further reutilization remains open.ResultsBioinformatic and experimental data presented in this paper indicate that two Arabidopsis staphylococcal-like nucleases, named CAN1 and CAN2, are anchored to the cell membrane via N-terminal myristoylation and palmitoylation modifications. Both proteins possess a unique hybrid structure in their catalytic domain consisting of staphylococcal nuclease-like and tRNA synthetase anticodon binding-like motifs. They are neutral, Ca2+-dependent nucleaces showing a different specificity toward the ssDNA, dsDNA and RNA substrates. A study of microarray experiments and endogenous nuclease activity revealed that expression of CAN1 gene correlates with different forms of programmed cell death, while the CAN2 gene is constitutively expressed.ConclusionsIn this paper we present evidence showing that two plant staphylococcal-like nucleases belong to a new, as yet unidentified class of eukaryotic nucleases, characterized by unique plasma membrane localization. The identification of this class of nucleases indicates that plant cells possess additional, so far uncharacterized, mechanisms responsible for DNA and RNA degradation. The potential functions of these nucleases in relation to their unique intracellular location are discussed.

show abstract

Tissue-specific organelle DNA degradation mediated by DPD1 exonuclease

Cited by 19 publications

References 16 publications

Mutations defective in ribonucleotide reductase activity interfere with pollen plastid DNA degradation mediated by DPD1 exonuclease

Mutations defective in ribonucleotide reductase activity interfere with pollen plastid DNA degradation mediated by DPD1 exonuclease

Genome-Wide Association Mapping of Loci Associated with Plant Growth and Forage Production under Salt Stress in Alfalfa (Medicago sativa L.)

Plant plasma membrane-bound staphylococcal-like DNases as a novel class of eukaryotic nucleases

Contact Info

Product

Resources

About