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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 3. Cover of RNA Biology Volume 9, Issue 12 (December 2012).
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Figure 3: Figure 3. Cover of RNA Biology Volume 9, Issue 12 (December 2012).

Mentions: In eukaryotic cells, many RNA species have to be exported from the nucleus to the cytoplasm. Different RNA species form distinct ribonucleoprotein (RNP) complexes for export, indicating specific RNA recognition by export proteins. Specific RNA recognition is usually achieved by specific RNA sequences or structures, but recently a new molecular mechanism by which the formation of export RNP complexes is specified by RNA length has been reported. RNA polymerase II (Pol II) is known to synthesize not only mRNAs but also shorter RNAs, including spliceosomal U snRNAs. Both types of RNAs initially acquire an m7G-cap structure at their 5′ends, to which the common factor cap-binding complex (CBC) binds. However, beyond this initial event, the subsequent assembly of their export complexes differs. Since neither class of RNAs contains clearly conserved RNA sequences or structures that could mediate this distinguishing features, Dr Mutsuhito Ohno set out to identify other special features of these RNAs that are recognized by the cellular RNA export machinery. Although the key U snRNA export factor, PHAX, could bind to mRNA in vitro, PHAX was excluded from mRNA in vivo. The heterotetramer of the heterogeneous nuclear RNP (hnRNP) C1/C2 specifically bound Pol II transcripts longer than 200–300nt, and funneled them into the mRNA export pathway by inhibiting their binding by PHAX, whereas shorter transcripts not bound by the heterotetramer were committed to the U snRNA export pathway. 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).3


Landes Highlights
Figure 3. Cover of RNA Biology Volume 9, Issue 12 (December 2012).
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 3: Figure 3. Cover of RNA Biology Volume 9, Issue 12 (December 2012).
Mentions: In eukaryotic cells, many RNA species have to be exported from the nucleus to the cytoplasm. Different RNA species form distinct ribonucleoprotein (RNP) complexes for export, indicating specific RNA recognition by export proteins. Specific RNA recognition is usually achieved by specific RNA sequences or structures, but recently a new molecular mechanism by which the formation of export RNP complexes is specified by RNA length has been reported. RNA polymerase II (Pol II) is known to synthesize not only mRNAs but also shorter RNAs, including spliceosomal U snRNAs. Both types of RNAs initially acquire an m7G-cap structure at their 5′ends, to which the common factor cap-binding complex (CBC) binds. However, beyond this initial event, the subsequent assembly of their export complexes differs. Since neither class of RNAs contains clearly conserved RNA sequences or structures that could mediate this distinguishing features, Dr Mutsuhito Ohno set out to identify other special features of these RNAs that are recognized by the cellular RNA export machinery. Although the key U snRNA export factor, PHAX, could bind to mRNA in vitro, PHAX was excluded from mRNA in vivo. The heterotetramer of the heterogeneous nuclear RNP (hnRNP) C1/C2 specifically bound Pol II transcripts longer than 200–300nt, and funneled them into the mRNA export pathway by inhibiting their binding by PHAX, whereas shorter transcripts not bound by the heterotetramer were committed to the U snRNA export pathway. 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).3

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.