Related ArticlesNMR investigations on H2A-H2B heterodimer dynamics conferred by histone variant H2A.Z.
Biochem Biophys Res Commun. 2019 10 22;518(4):752-758
Authors: Dai L, Xu N, Zhou Z
Abstract
H2A.Z, a highly conserved histone H2A variant in eukaryotes, plays critical roles in multiple nuclear events. H2A.Z forms a heterodimer with H2B when incorporated into nucleosomes. The heterodimer dynamics has been implicated in H2A.Z functions. To gain insights into H2A.Z dynamics, we analyzed yeast H2A.Z-H2B dimer (ZB) and yeast H2A-H2B dimer (AB) using solution NMR spectroscopy. First, we measured the 1H-15N heteronuclear NOE ratio of ZB and showed that the H2A.Z ?C-helix region (residues 100-118) undergoes less structure fluctuation than its H2A counterpart. Strikingly, substituting H2A residues G99N100V101 with H2A.Z counterparts R106A107 reduced the fluctuation of H2A ?C-helix, suggesting that H2A.Z dynamics play an important role in ?C-helix extension and H2A.Z-chaperones recognition. We next measured the hydrogen-deuterium exchange (HX) rate of ZB and verified that the H2A.Z ?2 helix and H2B ?2, ?3 helices are mostly protected. Notably, we observed nearly identical HX profiles for dimerized ZB and AB, suggesting that they have similar solution structures and dynamic characters. Together, our study gains first insight into H2A.Z-H2B dimer dynamics and sheds light on how its dynamics affect the structure and function of H2A.Z variant.
Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c 552 and its b -type variant
Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c 552 and its b -type variant
Abstract
Cytochrome c 552 from the thermophilic bacterium Hydrogenobacter thermophilus is a typical c-type cytochrome which binds heme covalently via two thioether bonds between the two heme vinyl groups and two cysteine thiol groups in a CXXCH sequence motif. This protein was converted to a b-type cytochrome by substitution of the two cysteine residues by alanines (Tomlinson and Ferguson in Proc Natl Acad Sci USA...
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[NMR paper] Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Angew Chem Int Ed Engl. 2013 Mar 11;52(11):3145-7
Authors: Werbeck ND, Kirkpatrick J,...
A topical issue: NMR investigations of molecular dynamics
A topical issue: NMR investigations of molecular dynamics
A topical issue: NMR investigations of molecular dynamics
Content Type Journal Article
Pages 1-4
DOI 10.1007/s10858-009-9345-8
Authors
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01-09-2011 12:46 PM
[NMR paper] NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop bin
NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop binding protein.
Related Articles NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop binding protein.
RNA. 2002 Jan;8(1):83-96
Authors: DeJong ES, Marzluff WF, Nikonowicz EP
The 3' end of replication-dependent histone mRNAs terminate in a conserved sequence containing a stem-loop. This 26-nt sequence is the binding site for a protein, stem-loop binding protein (SLBP), that is involved in multiple aspects of histone mRNA metabolism...
NMR investigations on H2A-H2B heterodimer dynamics conferred by histone variant H2A.Z.
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