Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

 
 
DownloadE-Mail
  Archaeal Histone Tetramerization Determines DNA Affinity and the Direction of DNA Supercoiling

Marc, F., Sandman, K. M., Lurz, R., & Reeve, J. N. (2002). Archaeal Histone Tetramerization Determines DNA Affinity and the Direction of DNA Supercoiling. Journal of Biological Chemistry, 277(34), 30879-30886.

Item is

Externe Referenzen

einblenden:

Urheber

einblenden:
ausblenden:
 Urheber:
Marc, Frédéric, Autor
Sandman, Kathleen M., Autor
Lurz, Rudi1, Autor
Reeve, John N., Autor
Affiliations:
1Max Planck Society, ou_persistent13              

Inhalt

einblenden:
ausblenden:
Schlagwörter: -
 Zusammenfassung: 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.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2002-06-10
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: eDoc: 24237
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Journal of Biological Chemistry
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 277 (34) Artikelnummer: - Start- / Endseite: 30879 - 30886 Identifikator: -