1yqa

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{{STRUCTURE_1yqa| PDB=1yqa | SCENE= }}
{{STRUCTURE_1yqa| PDB=1yqa | SCENE= }}
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'''Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p'''
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===Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p===
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==Overview==
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Yeast Hho1p contains two domains, GI and GII, that are homologous to the single globular domain of the linker histone H1 (GH1). We showed previously that the isolated GI and GII domains have different structural stabilities and functional properties. GI, like GH1 and the related GH5, is stably folded at low ionic strength (10 mM sodium phosphate) and gives strong protection of chromatosome-length DNA ( approximately 166 bp) during micrococcal nuclease digestion of chromatin. GII is intrinsically unfolded in 10 mM sodium phosphate and gives weak chromatosome protection, but in 250 mM sodium phosphate has a structure very similar to that of GI as determined by NMR spectroscopy. We now show that the loop between helices II and III in GII is the cause of both its instability and its inability to confer strong chromatosome protection. A mutant GII, containing the loop of GI, termed GII-L, is stable in 10 mM sodium phosphate and is as effective as GI in chromatosome protection. Two GII mutants with selected mutations within the original loop were also slightly more stable than GII. In GII, two of the four basic residues conserved at the second DNA binding site ("site II") on the globular domain of canonical linker histones, and in GI, are absent. Introduction of the two "missing" site II basic residues into GII or GII-L destabilised the protein and led to decreased chromatosome protection relative to the protein without the basic residues. In general, the ability to confer chromatosome protection in vitro is closely related to structural stability (the relative population of structured and unstructured states). We have determined the structure of GII-L by NMR spectroscopy. GII-L is very similar to GII folded in 250 mM sodium phosphate, with the exception of the substituted loop region, which, as in GI, contains a single helical turn.
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{{ABSTRACT_PUBMED_15878177}}
==About this Structure==
==About this Structure==
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1YQA 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=1YQA OCA].
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1YQA 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=1YQA OCA].
==Reference==
==Reference==
Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p., Sanderson A, Stott K, Stevens TJ, Thomas JO, J Mol Biol. 2005 Jun 10;349(3):608-20. Epub 2005 Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15878177 15878177]
Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p., Sanderson A, Stott K, Stevens TJ, Thomas JO, J Mol Biol. 2005 Jun 10;349(3):608-20. Epub 2005 Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15878177 15878177]
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Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p., Ali T, Coles P, Stevens TJ, Stott K, Thomas JO, J Mol Biol. 2004 Apr 16;338(1):139-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15050829 15050829]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Thomas, J O.]]
[[Category: Thomas, J O.]]
[[Category: Winged-helix]]
[[Category: Winged-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:26:42 2008''

Revision as of 02:26, 29 July 2008

Image:1yqa.png

Template:STRUCTURE 1yqa

Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p

Template:ABSTRACT PUBMED 15878177

About this Structure

1YQA is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.

Reference

Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p., Sanderson A, Stott K, Stevens TJ, Thomas JO, J Mol Biol. 2005 Jun 10;349(3):608-20. Epub 2005 Apr 19. PMID:15878177

Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p., Ali T, Coles P, Stevens TJ, Stott K, Thomas JO, J Mol Biol. 2004 Apr 16;338(1):139-48. PMID:15050829

Page seeded by OCA on Tue Jul 29 05:26:42 2008

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