NAC transcription factor: Difference between revisions

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The transcription regulatory region, generally lying at the highly diverged C-terminal, can either activate  <ref>http://www.plantcell.org/content/16/9/2481.full.pdf+html</ref> <ref>http://onlinelibrary.wiley.com/doi/10.1111/j.1365-313X.2005.02575.x/pdf</ref> <ref>http://www.springerlink.com/content/8101522211447210/fulltext.pdf</ref> or repress transcription  <ref name="plantc">http://www.plantcell.org/content/22/4/1249.full.pdf+html</ref> <ref name="jbc">http://www.jbc.org/content/282/50/36292.full.pdf</ref> <ref>http://onlinelibrary.wiley.com/doi/10.1111/j.1365-313X.2005.02488.x/pdf</ref>. Recently, the C-terminal of a novel  NAC domain protein VNI have been shown to both activate and repress transcription  <ref>http://www.plantcell.org/content/early/2011/06/13/tpc.111.084913.full.pdf+html</ref>. More interestingly, VNI2 transcriptional repression motif can be transformed into the transcription activation domain under high salt conditions. It is therefore likely that the C-terminal domain isn’t only complex in sequence, but confer  the multiple functions.  Based on the sequence analyses, the transcription regulatory region has several  group specific motifs that are rich in repeats of serine–threonine, proline–glutamine, or acidic residues, for example, the transcription regulatory region of rice NAC proteins was found to contain ten C-terminal motifs  <ref>http://www.biomedcentral.com/content/pdf/1756-0500-4-302.pdf</ref>. Another comprehensive study has revealed that these motifs are conserved for a given subgroup of NAC subfamilies but varies across the different subfamilies<ref name="oxford">http://mplant.oxfordjournals.org/content/early/2011/12/01/mp.ssr098.full.pdf+html
The transcription regulatory region, generally lying at the highly diverged C-terminal, can either activate  <ref>http://www.plantcell.org/content/16/9/2481.full.pdf+html</ref> <ref>http://onlinelibrary.wiley.com/doi/10.1111/j.1365-313X.2005.02575.x/pdf</ref> <ref>http://www.springerlink.com/content/8101522211447210/fulltext.pdf</ref> or repress transcription  <ref name="plantc">http://www.plantcell.org/content/22/4/1249.full.pdf+html</ref> <ref name="jbc">http://www.jbc.org/content/282/50/36292.full.pdf</ref> <ref>http://onlinelibrary.wiley.com/doi/10.1111/j.1365-313X.2005.02488.x/pdf</ref>. Recently, the C-terminal of a novel  NAC domain protein VNI have been shown to both activate and repress transcription  <ref>http://www.plantcell.org/content/early/2011/06/13/tpc.111.084913.full.pdf+html</ref>. More interestingly, VNI2 transcriptional repression motif can be transformed into the transcription activation domain under high salt conditions. It is therefore likely that the C-terminal domain isn’t only complex in sequence, but confer  the multiple functions.  Based on the sequence analyses, the transcription regulatory region has several  group specific motifs that are rich in repeats of serine–threonine, proline–glutamine, or acidic residues, for example, the transcription regulatory region of rice NAC proteins was found to contain ten C-terminal motifs  <ref>http://www.biomedcentral.com/content/pdf/1756-0500-4-302.pdf</ref>. Another comprehensive study has revealed that these motifs are conserved for a given subgroup of NAC subfamilies but varies across the different subfamilies<ref name="oxford">http://mplant.oxfordjournals.org/content/early/2011/12/01/mp.ssr098.full.pdf+html
</ref>. Thus, this region imparts variation to individual functions of NAC proteins. Additionally, because of the excessive low-complexity sequences, transcription regulatory regions have a high degree of intrinsic disorder (ID) and fail to have a single stable three-dimensional structure <ref name="content">http://www.jbc.org/content/286/41/35418.full.pdf+html</ref><ref>http://peer.ccsd.cnrs.fr/docs/00/47/92/44/PDF/PEER_stage2_10.1042%252FBJ20091234.pdf</ref>. Such flexibility enables them to interact with different target proteins making them model proteins for systematic analysis of transcription factor functions and structural ID. Some NAC proteins have protein-binding ability in their TRRs  <ref name="jbc">http://www.jbc.org/content/282/50/36292.full.pdf</ref>  <ref name="content">http://www.jbc.org/content/286/41/35418.full.pdf+html</ref> <ref name="mpiz">http://www.mpiz-koeln.mpg.de/26442/Kleinow_Plant_J_23_pdf.pdf</ref>. An a-helical transmembrane (TM) motif present in some NAC proteins is responsible for plasma membrane or endoplasmic reticulum membrane anchoring  <ref name="mpiz">http://www.mpiz-koeln.mpg.de/26442/Kleinow_Plant_J_23_pdf.pdf</ref>. Up to now, 18 membrane bound NAC proteins have been identified in Arabidopsis, 11 in soybean, seven in maize (Zea mays), six in grape, five each in rice, poplar, switchgrass (Panicum virgatum) and sorghum (Sorghum bicolor), and four in Medicago truncatula  <ref> http://signet.korea.ac.kr/webzine/6th/papers/Trends_in_Plant_Science_200810.pdf</ref> <ref>http://ac.els-cdn.com/S0888754309002122/1-s2.0-S0888754309002122-main.pdf?_tid=f675eda8581767131107a56c803e8434&acdnat=1336012303_7e1cc13e64dad88ebd90823905b9ccfb</ref>[31,32], which may play important regulatory roles under environmental cues. However, no VNDs and other NAC proteins relating to cell wall were identified to have transmembrane motif.
</ref>. Thus, this region imparts variation to individual functions of NAC proteins. Additionally, because of the excessive low-complexity sequences, transcription regulatory regions have a high degree of intrinsic disorder (ID) and fail to have a single stable three-dimensional structure <ref name="content">http://www.jbc.org/content/286/41/35418.full.pdf+html</ref><ref>http://peer.ccsd.cnrs.fr/docs/00/47/92/44/PDF/PEER_stage2_10.1042%252FBJ20091234.pdf</ref>. Such flexibility enables them to interact with different target proteins making them model proteins for systematic analysis of transcription factor functions and structural ID. Some NAC proteins have protein-binding ability in their TRRs  <ref name="jbc">http://www.jbc.org/content/282/50/36292.full.pdf</ref>  <ref name="content">http://www.jbc.org/content/286/41/35418.full.pdf+html</ref> <ref name="mpiz">http://www.mpiz-koeln.mpg.de/26442/Kleinow_Plant_J_23_pdf.pdf</ref>. An a-helical transmembrane (TM) motif present in some NAC proteins is responsible for plasma membrane or endoplasmic reticulum membrane anchoring  <ref name="mpiz">http://www.mpiz-koeln.mpg.de/26442/Kleinow_Plant_J_23_pdf.pdf</ref>. Up to now, 18 membrane bound NAC proteins have been identified in Arabidopsis, 11 in soybean, seven in maize (Zea mays), six in grape, five each in rice, poplar, switchgrass (Panicum virgatum) and sorghum (Sorghum bicolor), and four in Medicago truncatula  <ref> http://signet.korea.ac.kr/webzine/6th/papers/Trends_in_Plant_Science_200810.pdf</ref> <ref>http://ac.els-cdn.com/S0888754309002122/1-s2.0-S0888754309002122-main.pdf?_tid=f675eda8581767131107a56c803e8434&acdnat=1336012303_7e1cc13e64dad88ebd90823905b9ccfb</ref>, which may play important regulatory roles under environmental cues. However, no VNDs and other NAC proteins relating to cell wall were identified to have transmembrane motif.




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