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One example are histone posttranslational modifications (PTMs), such as acetylation, methylation, phosphorylation and ubiquitination... These marks function as signals during various chromatin-based processes and act as platforms for recruitment, assembly or retention of chromatin-associated factors... The key roles played by this histone mark in DNA repair, transcription and chromatin compaction during cell division and apoptosis are discussed... This finding revealed a novel function of the C1/C2 heterotetramer and highlighted the biological importance of RNA recognition by length... In a recent Point-of-View, Dr Ohno discusses questions raised by these results, together with some historical background of this finding (Fig.  3)... Dr Feng Gong and colleagues identified a deubiquitinating enzyme, USP24, as a likely DDB2-interacting protein... Interaction between DDB2 and USP24 was confirmed by co-precipitation... Importantly, knockdown of USP24 in two human cell lines decreased the steady-state levels of DDB2, indicating that USP24-mediated DDB2 deubiquitination prevents DDB2 degradation... In addition, the authors demonstrated that USP24 can cleave an ubiquitinated form of DDB2 in vitro... Taken together, these results suggest that the ubiquitin-specific protease USP24 is a novel regulator of DDB2 stability (Fig.  4).

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Figure 2. Cover of Plant Signaling and Behavior Volume 7, Issue 10 (October 2012).
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Figure 2: Figure 2. Cover of Plant Signaling and Behavior Volume 7, Issue 10 (October 2012).

Mentions: Plants use sophisticated defense systems against pathogen infection. Cellular resistance signaling involves the transduction of stress stimuli into the nucleus to reprogram the expression pattern of defense genes and subsequent export of transcripts for protein biosynthesis in the cytoplasm mediating an appropriate immune response. Nuclear pore complexes (NPCs), composed of various nucleoporins (Nups), mediate the regulated exchange of proteins and RNAs between the cytoplasm and the nucleus. A previous study investigated in a reverse-genetics approach whether members of the Arabidopsis Nup 107–160 nuclear pore sub-complex are required for plant immunity. Results showed that plants carrying mutations in components of this complex, Nup160 and Seh1, are compromised in basal resistance to virulent Pseudomonas bacteria. Both genes also contributed to immunity conferred by Toll interleukin 1 receptor/nucleotide-binding/leucine-rich repeat (TNL)-type R proteins and to constitutive resistance activated in a deregulated TNL mutant, snc1. Protein levels of EDS1, a central regulator of TNL-triggered resistance, were reduced in seh1 and severely depleted in nup160 single mutants. Following up on these previous findings, Drs Roth and Wiermer investigated the impact of mutations in Nup160, Seh1 and a third complex member, MOS3/Nup96, on EDS1 protein accumulation in the snc1 auto-immune mutant background. In addition, they examined the subcellular localization of Seh1 in root tissues. The study results suggest that Nup160 and Seh1 differently affect TNL-type R protein triggered resistance and auto-immunity in snc1 mutants, possibly because of the different subcellular localization of the proteins or due to partial compensation of Seh1-linked defects by Nup160 or other Nups (Fig. 2).2


Landes Highlights
Figure 2. Cover of Plant Signaling and Behavior Volume 7, Issue 10 (October 2012).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3585020&req=5

Figure 2: Figure 2. Cover of Plant Signaling and Behavior Volume 7, Issue 10 (October 2012).
Mentions: Plants use sophisticated defense systems against pathogen infection. Cellular resistance signaling involves the transduction of stress stimuli into the nucleus to reprogram the expression pattern of defense genes and subsequent export of transcripts for protein biosynthesis in the cytoplasm mediating an appropriate immune response. Nuclear pore complexes (NPCs), composed of various nucleoporins (Nups), mediate the regulated exchange of proteins and RNAs between the cytoplasm and the nucleus. A previous study investigated in a reverse-genetics approach whether members of the Arabidopsis Nup 107–160 nuclear pore sub-complex are required for plant immunity. Results showed that plants carrying mutations in components of this complex, Nup160 and Seh1, are compromised in basal resistance to virulent Pseudomonas bacteria. Both genes also contributed to immunity conferred by Toll interleukin 1 receptor/nucleotide-binding/leucine-rich repeat (TNL)-type R proteins and to constitutive resistance activated in a deregulated TNL mutant, snc1. Protein levels of EDS1, a central regulator of TNL-triggered resistance, were reduced in seh1 and severely depleted in nup160 single mutants. Following up on these previous findings, Drs Roth and Wiermer investigated the impact of mutations in Nup160, Seh1 and a third complex member, MOS3/Nup96, on EDS1 protein accumulation in the snc1 auto-immune mutant background. In addition, they examined the subcellular localization of Seh1 in root tissues. The study results suggest that Nup160 and Seh1 differently affect TNL-type R protein triggered resistance and auto-immunity in snc1 mutants, possibly because of the different subcellular localization of the proteins or due to partial compensation of Seh1-linked defects by Nup160 or other Nups (Fig. 2).2

View Article: PubMed Central

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

One example are histone posttranslational modifications (PTMs), such as acetylation, methylation, phosphorylation and ubiquitination... These marks function as signals during various chromatin-based processes and act as platforms for recruitment, assembly or retention of chromatin-associated factors... The key roles played by this histone mark in DNA repair, transcription and chromatin compaction during cell division and apoptosis are discussed... This finding revealed a novel function of the C1/C2 heterotetramer and highlighted the biological importance of RNA recognition by length... In a recent Point-of-View, Dr Ohno discusses questions raised by these results, together with some historical background of this finding (Fig.  3)... Dr Feng Gong and colleagues identified a deubiquitinating enzyme, USP24, as a likely DDB2-interacting protein... Interaction between DDB2 and USP24 was confirmed by co-precipitation... Importantly, knockdown of USP24 in two human cell lines decreased the steady-state levels of DDB2, indicating that USP24-mediated DDB2 deubiquitination prevents DDB2 degradation... In addition, the authors demonstrated that USP24 can cleave an ubiquitinated form of DDB2 in vitro... Taken together, these results suggest that the ubiquitin-specific protease USP24 is a novel regulator of DDB2 stability (Fig.  4).

No MeSH data available.