Atomic force microscopy of nucleoprotein complexes.

Détails

ID Serval
serval:BIB_BC7EDE6F728D
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Institution
Titre
Atomic force microscopy of nucleoprotein complexes.
Périodique
Scanning Microscopy
Auteur(s)
Lyubchenko Y.L., Jacobs B.L., Lindsay S.M., Stasiak A.
ISSN
0891-7035[print], 0891-7035[linking]
Statut éditorial
Publié
Date de publication
09/1995
Volume
9
Numéro
3
Pages
705-24; discussion 724-7
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
Publication Status: ppublish
Résumé
Recent data on the AFM studies of nucleoprotein complexes of different types are reviewed in this paper. The first section describes the progress in the sample preparation methods for AFM studies of nucleic acids and nucleoprotein complexes. The second part of this paper reviews AFM data on studies of complexes of DNA with regulatory proteins. These studies include two different types of DNA distortion induced by proteins binding: local bending of DNA at sites of protein binding and formation of large loops due to protein-protein interactions between molecules bound to distant sites along the DNA molecules (DNA looping). The prospects for use of AFM for physical mapping of genomes are discussed in this section as well. The third part of the paper reviews data on studies of complexes of DNA with non-sequence specific binding proteins. Special emphasis is given to studies of chromatin which have resulted in progress in the understanding of structure of native chromatin fiber. In this section, novel data on AFM studies of RecA-DNA filaments and complexes of dsRNA with the dsRNA-specific protein p25 are also presented. Discussion of the substrate preparation procedures in relation to the AFM studies of nucleoprotein complexes is given in the final section.
Mots-clé
Animals, Bacteriophages/isolation &amp, purification, Chromatin/ultrastructure, DNA/chemistry, Humans, Microscopy, Atomic Force, Nucleoproteins/analysis, RNA, Double-Stranded/chemistry
Pubmed
Web of science
Création de la notice
24/01/2008 11:36
Dernière modification de la notice
20/08/2019 16:30
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