Atomic force microscopy of nucleoprotein complexes.
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.
Lyubchenko
Y L
YL
Department of Microbiology, Arizona State University, Tempe 85287-2701, USA.
Jacobs
B L
BL
Lindsay
S M
SM
Stasiak
A
A
D000818:Animals; D001435:Bacteriophages / Q000302:isolation & purification; D002843:Chromatin / Q000648:ultrastructure; D004247:DNA / Q000737:chemistry; D006801:Humans; D018625:Microscopy, Atomic Force; D009698:Nucleoproteins / Q000032:analysis*; D012330:RNA, Double-Stranded / Q000737:chemistry
D002843:Chromatin; D009698:Nucleoproteins; D012330:RNA, Double-Stranded; D004247:DNA