HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 277, Issue 34, 30879-30886, August 23, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/34/30879    most recent M203674200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Marc, F. Articles by Reeve, J. N. Search for Related Content PubMed PubMed Citation Articles by Marc, F. Articles by Reeve, J. N. Social Bookmarking                      What's this?

Archaeal Histone Tetramerization Determines DNA Affinity and the Direction of DNA Supercoiling^*

Frédéric Marc^§, Kathleen Sandman^§, Rudi Lurz^¶, and John N. Reeve

From the  Department of Microbiology, Ohio State University, Columbus, Ohio 43210 and the ^¶ Max Planck Institut für Molekulare Genetik, D-14195, Berlin-Dahlem, Germany

DNA binding and the topology of DNA have been determined in complexes formed by >20 archaeal histone variants and archaeal histone dimer fusions with residue replacements at sites responsible for histone fold dimer:dimer interactions. Almost all of these variants have decreased affinity for DNA. They have also lost the flexibility of the wild type archaeal histones to wrap DNA into a negative or positive supercoil depending on the salt environment; they wrap DNA into positive supercoils under all salt conditions. The histone folds of the archaeal histones, HMfA and HMfB, from Methanothermus fervidus are almost identical, but (HMfA)₂ and (HMfB)₂ homodimers assemble into tetramers with sequence-dependent differences in DNA affinity. By construction and mutagenesis of HMfA+HMfB and HMfB+HMfA histone dimer fusions, the structure formed at the histone dimer:dimer interface within an archaeal histone tetramer has been shown to determine this difference in DNA affinity. Therefore, by regulating the assembly of different archaeal histone dimers into tetramers that have different sequence affinities, the assembly of archaeal histone-DNA complexes could be localized and used to regulate gene expression.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				U. Friedrich-Jahn, J. Aigner, G. Langst, J. N. Reeve, and H. Huber Nanoarchaeal Origin of Histone H3? J. Bacteriol., February 1, 2009; 191(3): 1092 - 1096. [Abstract] [Full Text] [PDF]

				A. Mukherjee, A. O. Sokunbi, and A. Grove DNA protection by histone-like protein HU from the hyperthermophilic eubacterium Thermotoga maritima Nucleic Acids Res., July 1, 2008; 36(12): 3956 - 3968. [Abstract] [Full Text] [PDF]

				Y. Xie and J. N. Reeve Transcription by an Archaeal RNA Polymerase Is Slowed but Not Blocked by an Archaeal Nucleosome J. Bacteriol., June 1, 2004; 186(11): 3492 - 3498. [Abstract] [Full Text] [PDF]

				D. J. Soares, F. Marc, and J. N. Reeve Conserved Eukaryotic Histone-Fold Residues Substituted into an Archaeal Histone Increase DNA Affinity but Reduce Complex Flexibility J. Bacteriol., June 1, 2003; 185(11): 3453 - 3457. [Abstract] [Full Text] [PDF]