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  Nucleosome-like complex of the histone from the hyperthermophile Methanopyrus kandleri (MkaH) with linear DNA

Pavlov, N. A., Cherny, D. I., Jovin, T. M., & Slesarev, A. I. (2002). Nucleosome-like complex of the histone from the hyperthermophile Methanopyrus kandleri (MkaH) with linear DNA. Journal of Biomolecular Structure & Dynamics, 20(2), 207-214. Retrieved from http://www.jbsdonline.com/download/11213.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F2DB-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-09A5-5
Genre: Journal Article

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Pavlov, N. A.1, Author              
Cherny, D. I.1, Author              
Jovin, T. M.1, Author              
Slesarev, A. I., Author
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1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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Free keywords: histone; nucleosome; hyperthermophile; Methanopyrus kandleri; DNA wrapping
 Abstract: The MkaH protein from the archaeon Methanopyrus kandleri, an unusual assembly of two histone-fold domains in a single polypeptide chain, demonstrates high structural similarity to eukaryal histories. We studied the DNA binding and self- association properties of MkaH by means of the electrophoretic mobility shift assay (EMSA), electron microscopy (EM), chemical cross-linking, and analytical gel filtration. EMSA showed an increased mobility of linear DNA complexed with MkaH protein with a maximum at a protein-DNA weight ratio (R-w) of approximate to 3; the mobility decreased at higher protein concentration. EM of the complexes formed at R-w less than or equal to 3 revealed formation of isometric loops encompassing 71 +/- 7 bp of DNA duplex. At high values of R-w (greater than or equal to9) thickened compact nucleoprotein structures were observed; no individual loops were seen within the complexes. Gel filtration chromatography and chemical fixation indicated that in the absence of DNA the dominant form of the MkaH in solution, unlike other archaeal histones, is a stable dimer (pseudo-tetramer of the histone-fold domain) apparently resembling the eukaryal (H3-H4)(2) tetramer. Similarly; dimers are the dominant form of the protein interacting with DNA. The properties of MkaH supporting the assignment of its intermediate position between other archaeal and eukaryal histones are discussed.

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Language(s): eng - English
 Dates: 2002-10
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Biomolecular Structure & Dynamics
Source Genre: Journal
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Pages: - Volume / Issue: 20 (2) Sequence Number: - Start / End Page: 207 - 214 Identifier: -