Mutational Analyses of a Fork Head Associated Domain Protein, DAWDLE, in &amp;lt;i&amp;gt;Arabidopsis thaliana&amp;lt;/i&amp;gt;

Narayanan, Lakshmi; Mukherjee, Dipaloke; Zhang, Shuxin; Yu, Bin; Chevalier, David

doi:10.4236/ajps.2014.518297

Cited by 4 publications

(2 citation statements)

References 19 publications

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“…This consists with the fact that DCL1 is phosphorylated . Furthermore, mutations in FHA domain can abolish the DDL–DCL1 interaction and impair miRNA maturation (Figure (b)), indicating that phosphorylation of DCL1 may be important for the DDL–DCL1 interaction and pri‐miRNA processing …”

Section: Regulation Of Pri‐mirna Processingmentioning

confidence: 95%

New insights into pri‐miRNA processing and accumulation in plants

Zhang

Liu

2015

WIREs RNA

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MicroRNAs (miRNAs) regulate many biological processes such as development, metabolism, and others. They are processed from their primary transcripts called primary miRNA transcripts (pri-miRNAs) by the processor complex containing the RNAse III enzyme, DICER-LIKE1 (DCL1), in plants. Consequently, miRNA biogenesis is controlled through altering pri-miRNA accumulation and processing, which is crucial for plant development and adaptation to environmental changes. Plant pri-miRNAs are transcribed by DNA-dependent RNA polymerase II (Pol II) and their levels are determined through transcription and degradation, whereas pri-miRNA processing is affected by its structure, splicing, alternative splicing, loading to the processor and the processor activity, which involve in many accessory proteins. Here, we summarize recent progresses related to pri-miRNA transcription, stability, and processing in plants.

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Section: Regulation Of Pri‐mirna Processingmentioning

confidence: 95%

New insights into pri‐miRNA processing and accumulation in plants

Zhang

Liu

2015

WIREs RNA

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“…Consistently, the PARylation sites are mainly located on DDL-N (Fig 6). DDL-N bears certain homology with proteins in RNA metabolism, and DDL possesses the RNA binding activity in vitro [21,32]. It remains unknown whether DDL PARylation mutants affect RNA binding activity.…”

Section: Discussionmentioning

confidence: 99%

PARylation of the forkhead‐associated domain protein DAWDLE regulates plant immunity

Feng

Chen

et al. 2016

EMBO Reports

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Protein poly(ADP-ribosyl)ation (PARylation) primarily catalyzed by poly(ADP-ribose) polymerases (PARPs) plays a crucial role in controlling various cellular responses. However, PARylation targets and their functions remain largely elusive. Here, we deployed an Arabidopsis protein microarray coupled with in vitro PARylation assays to globally identify PARylation targets in plants. Consistent with the essential role of PARylation in plant immunity, the forkhead-associated (FHA) domain protein DAWDLE (DDL), one of PARP2 targets, positively regulates plant defense to both adapted and non-adapted pathogens. Arabidopsis PARP2 interacts with and PARylates DDL, which was enhanced upon treatment of bacterial flagellin. Mass spectrometry and mutagenesis analysis identified multiple PARylation sites of DDL by PARP2. Genetic complementation assays indicate that DDL PARylation is required for its function in plant immunity. In contrast, DDL PARylation appears to be dispensable for its previously reported function in plant development partially mediated by the regulation of microRNA biogenesis. Our study uncovers many previously unknown PARylation targets and points to the distinct functions of DDL in plant immunity and development mediated by protein PARylation and small RNA biogenesis, respectively.

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The role of forkhead-associated (FHA)-domain proteins in plant biology

Wang

2023

Plant Mol Biol

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Mutational Analyses of a Fork Head Associated Domain Protein, DAWDLE, in <i>Arabidopsis thaliana</i>

Cited by 4 publications

References 19 publications

New insights into pri‐miRNA processing and accumulation in plants

New insights into pri‐miRNA processing and accumulation in plants

PARylation of the forkhead‐associated domain protein DAWDLE regulates plant immunity

The role of forkhead-associated (FHA)-domain proteins in plant biology

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