5-Formylcytosine (5fC) is an endogenous DNA modification frequently found within regulatory elements of mammalian genes. Although 5fC is an oxidation product of 5-methylcytosine (5mC), the two epigenetic marks show distinct genome-wide distributions and protein affinities, suggesting that they perform different functions in epigenetic signaling. A unique feature of 5fC is the presence of a potentially reactive aldehyde group in its structure. Here, we show that 5fC bases in DNA readily form Schiff base conjugates with Lys side chains of nuclear proteins in vitro and in vivo. These covalent protein-DNA complexes are reversible (t1/2, 1.8 h), suggesting that they contribute to transcriptional regulation and chromatin remodeling. On the other hand, 5fC mediated DNA-protein cross-links, if present at replication forks or actively transcribed regions, may interfere with DNA replication and transcription.
Use of Protein Cross-Linking and Radiolytic LabelingTo Elucidate the Structure of PsbO withinHigher-Plant Photosystem II
Use of Protein Cross-Linking and Radiolytic LabelingTo Elucidate the Structure of PsbO withinHigher-Plant Photosystem II
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00365/20160603/images/medium/bi-2016-003659_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00365
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06-04-2016 11:08 AM
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry - Nature.com
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry - Nature.com
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Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry
Nature.com
We describe an integrated workflow that robustly identifies cross-links from endogenous protein complexes in human cellular lysates. Our approach is based on the application of mass spectrometry (MS)-cleavable cross-linkers,...
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09-29-2015 07:59 AM
Langerin–HeparinInteraction: Two Binding Sitesfor Small and Large Ligands As Revealed by a Combination of NMR Spectroscopyand Cross-Linking Mapping Experiments
Langerin–HeparinInteraction: Two Binding Sitesfor Small and Large Ligands As Revealed by a Combination of NMR Spectroscopyand Cross-Linking Mapping Experiments
Juan C. Mun?oz-Garci?a, Eric Chabrol, Romain R. Vive?s, Aline Thomas, Jose? L. de Paz, Javier Rojo, Anne Imberty, Franck Fieschi, Pedro M. Nieto and Jesu?s Angulo
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja511529x/20150319/images/medium/ja-2014-11529x_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja511529x...
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[NMR paper] Langerin-Heparin Interaction: Two Binding Sites for Small and Large Ligands as revealed by a combination of NMR Spectroscopy and Cross-Linking Mapping Experiments.
Langerin-Heparin Interaction: Two Binding Sites for Small and Large Ligands as revealed by a combination of NMR Spectroscopy and Cross-Linking Mapping Experiments.
Related Articles Langerin-Heparin Interaction: Two Binding Sites for Small and Large Ligands as revealed by a combination of NMR Spectroscopy and Cross-Linking Mapping Experiments.
J Am Chem Soc. 2015 Mar 6;
Authors: Muñoz-García JC, Chabrol E, Vives RR, Thomas A, de Paz JL, Rojo J, Imberty A, Fieschi F, Nieto PM, Angulo J
Abstract
Langerin is a C-type lectin present...
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[NMR paper] A new glycation product 'norpronyl-lysine' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
A new glycation product 'norpronyl-lysine' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
Related Articles A new glycation product 'norpronyl-lysine' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
Biosci Rep. 2014 Feb 12;
Authors: Bullock PT, Reid DG, Chow WY, Lau WP, Duer MJ
Abstract
NMR is ideal for characterizing non-enzymatic protein glycation, including AGEs (advanced glycation end products) underlying...
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Interactions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
Interactions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi102012j/aop/images/medium/bi-2010-02012j_0006.gif
Biochemistry
DOI: 10.1021/bi102012j
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03-09-2011 04:19 AM
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Biochemistry. 2011 Feb 16;
Authors: Mealman TD, Bagai I, Singh P, Goodlet DR, Rensing C, Zhou H, Wysocki VH, McEvoy MM
The E. coli periplasmic proteins CusF and CusB, as part of the CusCFBA efflux system, aid in the resistance of elevated levels of copper and silver by direct metal transfer between the...
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Effect of protein structural integrity on cross-linking by tyrosinase evidenced by mu
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear NMR spectroscopy.
J Biotechnol. 2010 Nov 15;
Authors: Hellman M, Mattinen ML, Fu B, Buchert J, Permi P
Enzymatic cross-linking of proteins can be catalyzed either by transferase-type enzymes, e.g., transglutaminases, or by oxidoreductases, e.g, tyrosinases or laccases. Three-dimensional structure of...