Related ArticlesNMR studies of translocation of the Zif268 protein between its target DNA sites.
Biochemistry. 2010 Aug 19;
Authors: Takayama Y, Sahu D, Iwahara J
Zif268 is a zinc-finger protein containing three Cys2-His2-type zinc-finger domains that bind the target DNA sequence GCGTGGGCG in a cooperative manner. In this work, we characterized translocation of the Zif268 protein between its target DNA sites using NMR spectroscopy. The residual dipolar coupling data and NMR chemical shift data suggested that the structure of the sequence-specific complex between Zif268 and its target DNA in solution is the same as the crystal structure. Using two-dimensional heteronuclear 1H-15N correlation spectra recorded with the fast acquisition method, we analyzed the kinetics of the process in which the Zif268 protein transfers from a target site to another on a different DNA molecule on a minute-hour timescale. By globally fitting the time-course data collected at some different DNA concentrations, we determined the dissociation rate constant for the specific complex and the second-order rate constant for direct transfer of Zif268 from one target site to another. Interestingly, direct transfer of the Zif268 protein between its target sites is >30,000-fold slower than corresponding direct transfers of the HoxD9 and the Oct-1 proteins, although the affinities of the three proteins to their target DNA sites are comparable. We also analyzed translocation of the Zif268 protein between two target sites on the same DNA molecules. The populations of the proteins bound to the target sites were found to depend on locations and orientations of the target sites.
PMID: 20718505 [PubMed - as supplied by publisher]
Exploring translocation of proteins on DNA by NMR
Exploring translocation of proteins on DNA by NMR
Abstract While an extensive body of knowledge has accumulated on the structures of transcription factors, DNA and their complexes from both NMR and crystallography, much less is known at a molecular level regarding the mechanisms whereby transcription factors locate their specific DNA target site within an overwhelming sea of non-specific DNA sites. Indirect kinetic data suggested that three processes are involved in the search procedure: jumping by dissociation of the protein from the DNA followed by re-association at another site,...
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Exploring translocation of proteins on DNA by NMR.
Exploring translocation of proteins on DNA by NMR.
Exploring translocation of proteins on DNA by NMR.
J Biomol NMR. 2011 Aug 17;
Authors: Marius Clore G
Abstract
While an extensive body of knowledge has accumulated on the structures of transcription factors, DNA and their complexes from both NMR and crystallography, much less is known at a molecular level regarding the mechanisms whereby transcription factors locate their specific DNA target site within an overwhelming sea of non-specific DNA sites. Indirect kinetic data suggested that...
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08-19-2011 02:56 PM
[NMR paper] Insights into the interactions between a drug and a membrane protein target by fluori
Insights into the interactions between a drug and a membrane protein target by fluorine cross-polarization magic angle spinning NMR.
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Magn Reson Chem. 2004 Feb;42(2):204-11
Authors: Boland MP, Middleton DA
The fluorinated anti-psychotic drug trifluoperazine (TFP) has been shown to be a K(+)-competitive inhibitor of gastric H(+)/K(+)-ATPase, a membrane-embedded therapeutic target for peptic ulcer...
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11-24-2010 09:25 PM
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
NMR backbone dynamics studies of human PED/PEA-15 outline protein functional sites.
FEBS J. 2010 Sep 3;
Authors: Farina B, Pirone L, Russo L, Viparelli F, Doti N, Pedone C, Pedone EM, Fattorusso R
PED/PEA-15 (phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes) is a ubiquitously expressed protein and a key regulator of cell growth and glucose metabolism. PED/PEA-15 mediates both homotypic and heterotypic interactions and is constituted by...
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NMR Studies of Translocation of the Zif268 Protein between Its Target DNA Sites
NMR Studies of Translocation of the Zif268 Protein between Its Target DNA Sites
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi100962h/aop/images/medium/bi-2010-00962h_0005.gifBiochemistry, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
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08-31-2010 10:50 PM
[NMR paper] Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spec
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Int J Pept Protein Res. 1996 Apr;47(4):282-8
Authors: Katahira R, Flotow H, Thomas G, Nosaka AY
An increase in the rate of protein synthesis is found to be accompanied by phosphorylation of the 40S ribosomal protein S6. Treatment of S6 by cyanogen bromide produced three fragments, and one of the fragments of S6, which is a C-terminal...
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[NMR paper] Initiation sites of protein folding by NMR analysis.
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Initiation sites of protein folding by NMR analysis.
Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10600-3
Authors: Freund SM, Wong KB, Fersht AR
Detailed characterization of denatured states of proteins is necessary to understand the interactions that funnel the large number of possible conformations along fast routes for folding. Nuclear magnetic resonance...
NMR studies of translocation of the Zif268 protein between its target DNA sites.
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