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{{STRUCTURE_2rnz|  PDB=2rnz  |  SCENE=  }}  
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'''Solution structure of the presumed chromodomain of the yeast histone acetyltransferase, Esa1'''
===Solution structure of the presumed chromodomain of the yeast histone acetyltransferase, Esa1===




==Overview==
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Chromodomains are methylated histone binding modules that have been widely studied. Interestingly, some chromodomains are reported to bind to RNA and/or DNA, although the molecular basis of their RNA/DNA interactions has not been solved. Here we propose a novel binding mode for chromodomain-RNA interactions. Essential Sas-related acetyltransferase 1 (Esa1) contains a presumed chromodomain in addition to a histone acetyltransferase domain. We initially determined the solution structure of the Esa1 presumed chromodomain and showed it to consist of a well-folded structure containing a five-stranded beta-barrel similar to the tudor domain rather than the canonical chromodomain. Furthermore, the domain showed no RNA/DNA binding ability. Because the N-terminus of the protein forms a helical turn, we prepared an N-terminally extended construct, which we surprisingly found to bind to poly(U) and to be critical for in vivo function. This extended protein contains an additional beta-sheet that acts as a knot for the tudor domain and binds to oligo(U) and oligo(C) with greater affinity compared with other oligo-RNAs and DNAs examined thus far. The knot does not cause a global change in the core structure but induces a well-defined loop in the tudor domain itself, which is responsible for RNA binding. We made 47 point mutants in an esa1 mutant gene in yeast in which amino acids of the Esa1 knotted tudor domain were substituted to alanine residues and their functional abilities were examined. Interestingly, the knotted tudor domain mutations that were lethal to the yeast lost poly(U) binding ability. Amino acids that are related to RNA interaction sites, as revealed by both NMR and affinity binding experiments, are found to be important in vivo. These findings are the first demonstration of how the novel structure of the knotted tudor domain impacts on RNA binding and how this influences in vivo function.
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==About this Structure==
==About this Structure==
2RNZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNZ OCA].  
2RNZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNZ OCA].  


==Reference==
==Reference==
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Tudor domain]]
[[Category: Tudor domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:22:59 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:34:31 2008''

Revision as of 00:34, 28 July 2008

File:2rnz.png

Template:STRUCTURE 2rnz

Solution structure of the presumed chromodomain of the yeast histone acetyltransferase, Esa1

Template:ABSTRACT PUBMED 18407291

About this Structure

2RNZ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.

Reference

Novel structural and functional mode of a knot essential for RNA binding activity of the Esa1 presumed chromodomain., Shimojo H, Sano N, Moriwaki Y, Okuda M, Horikoshi M, Nishimura Y, J Mol Biol. 2008 May 16;378(5):987-1001. Epub 2008 Mar 19. PMID:18407291

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