NAC transcription factor: Difference between revisions

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OCA, Hao Chen, David Canner, Michal Harel, Jaime Prilusky, Alexander Berchansky

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 == 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 [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebcterium diphtheria][http://en.wikipedia.org/wiki/X-ray_crystallography] 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 name="ncbi">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>. The NAC domain-fold also modulates dimerization through Leu14–Thr23 and Glu26–Tyr31 residues, which form a short antiparallel b-sheet at the dimer
+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. [http://en.wikipedia.org/wiki/X-ray_crystallography] 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 name="ncbi">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>. The 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 name ="nature">http://www.nature.com/embor/journal/v5/n3/pdf/7400093.pdf</ref> <ref name="ncbi">www.ncbi.nlm.nih.gov/pubmed/21337010</ref>  . This domain also contains mono or bipartite nuclear localization signals with the lysine residues in subdomain D playing crucial roles for nuclear shuttling  <ref name="MPLANT">http://www.springerlink.com/content/qq1584g690243n16/fulltext.pdf
 </ref> <ref>http://www.springerlink.com/content/r27215773758j405/fulltext.pdf</ref>.