NAC transcription factor: Difference between revisions
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== Conserved NAC domain == | == Conserved NAC domain == | ||
The DNA binding activity of NAC proteins is restricted into NAC domain which was divided into five subdomains A-E. The highly conserved positively charged subdomains C and D bind to DNA, whereas subdomain A may be involved in the formation of a functional dimer. X-ray crystallograhy have exhibited the presence of a novel transcription factor fold consisting of a twirled antiparallel β-sheet (β 1-6/7) which is used for DNA binding,located between an N-terminal helix and a short helix <ref>www.ncbi.nlm.nih.gov/pubmed/21337010</ref> <ref></ref>. Most importantly, Val119-Ser183, lys123 and lys126, along with Lys79, Arg85,and Arg 88 were identified as biochemically crucial for DNA binding. Arg88 is conserved in all NAC proteins but Lys79 and Arg85 could be exchangable but exert different DNA binding affinity | The DNA binding activity of NAC proteins is restricted into NAC domain which was divided into five subdomains A-E. The highly conserved positively charged subdomains C and D bind to DNA, whereas subdomain A may be involved in the formation of a functional dimer. X-ray crystallograhy have exhibited the presence of a novel transcription factor fold consisting of a twirled antiparallel β-sheet (β 1-6/7) which is used for DNA binding,located between an N-terminal helix and a short helix <ref>www.ncbi.nlm.nih.gov/pubmed/21337010</ref> <ref>http://www.springerlink.com/content/8p88600115713107/fulltext.pdf</ref>. Most importantly, Val119-Ser183, lys123 and lys126, along with Lys79, Arg85,and Arg 88 were identified as biochemically crucial for DNA binding. Arg88 is conserved in all NAC proteins but Lys79 and Arg85 could be exchangable but exert different DNA binding affinity <ref>http://www.springerlink.com/content/r27215773758j405/fulltext.pdf</ref>. TThe NAC domain-fold also modulates dimerization through Leu14–Thr23 and Glu26–Tyr31 residues, which form a short antiparallel b-sheet at the dimer | ||
interface stabilized by salt bridges formed by Arg19 and Glu26 <ref></ref> <ref></ref>[6,7]. This domain also contains mono or bipartite nuclear localization signals with the lysine residues in subdomain D playing crucial roles for nuclear shuttling <ref></ref> <ref></ref>[3,10]. | interface stabilized by salt bridges formed by Arg19 and Glu26 <ref></ref> <ref></ref>[6,7]. This domain also contains mono or bipartite nuclear localization signals with the lysine residues in subdomain D playing crucial roles for nuclear shuttling <ref></ref> <ref></ref>[3,10]. | ||
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*7.Chen et al(2011)A structual view of the conserved domain of rice stress-responsive NAC1. Protein cell 2, 55-63 http://www.springerlink.com/content/t567431215j02gu6/fulltext.pdf | *7.Chen et al(2011)A structual view of the conserved domain of rice stress-responsive NAC1. Protein cell 2, 55-63 http://www.springerlink.com/content/t567431215j02gu6/fulltext.pdf | ||
*8.Puranik et al. (2011) Molecular cloning and characterization of a membrane associated NAC family gene, SiNAC from foxtail millet. Mol. Biotech.49,138-150. | *8.Puranik et al. (2011) Molecular cloning and characterization of a membrane associated NAC family gene, SiNAC from foxtail millet. Mol. Biotech.49,138-150. http://www.springerlink.com/content/8p88600115713107/fulltext.pdf | ||
*9.Tran,L.S.P et al. (2009) Molecular characterization of stress-inducable GmNAC genes in soybean.Mol. Genet.Genomics 281.647-664. | *9.Tran,L.S.P et al. (2009) Molecular characterization of stress-inducable GmNAC genes in soybean.Mol. Genet.Genomics 281.647-664. http://www.springerlink.com/content/r27215773758j405/fulltext.pdf | ||
*10.Le, D.T. et al. (2011) Genome-wide survey and expression analysis of the plant-specific NAC transcription factor family in soybean during development and dehydration stress. DNA Res. 18, 263–276 | *10.Le, D.T. et al. (2011) Genome-wide survey and expression analysis of the plant-specific NAC transcription factor family in soybean during development and dehydration stress. DNA Res. 18, 263–276 | ||
