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Atomic Force Microscopy (Afm) of Chromatin Fibers: What Can We Learn?

Published online by Cambridge University Press:  02 July 2020

S.H. Leuba ,
R. Bash ,
D. Lohr ,
S. M. Lindsay  and
J. Zlatanova
S.H. Leuba
Affiliation:
Physical Molecular Biology, LRBGE, NCI, NIH, Bethesda, MD20892-5055;, leuba@nih.gov
R. Bash
Affiliation:
Arizona State University, Tempe, AZ85287-1504;, stuart.lindsay@asu.edu
D. Lohr
Affiliation:
Arizona State University, Tempe, AZ85287-1504;, stuart.lindsay@asu.edu
S. M. Lindsay
Affiliation:
Arizona State University, Tempe, AZ85287-1504;, stuart.lindsay@asu.edu
J. Zlatanova
Affiliation:
Argonne National Laboratory, Argonne, IL60439;, zlatanoj@everest.bim.anl.gov
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Extract

DNA in the eukaryotic nucleus is not naked. Instead, it is complexed at frequent intervals with an equal molecular mass of histones to form nucleosomes. In the nucleosome, ∼146 bp of DNA are wrapped around a core histone octamer composed of two copies each of histones H4, H3, H2B, and H2A. The family of linker histones (H1, H5 and H1°) bind to the DNA between successive nucleosomes and help maintain the three-dimensional arrangement of nucleosomes within the chromatin fiber. AFM studies of chromatin fibers with the histones either selectively trypsinized or selectively reconstituted demonstrate a specific role for the H3 N-termini in maintaining fiber structure, in conjunction with the 80 amino acid linker histone globular domain. These AFM results structurally agree with the location of the H3 N-termini in the histone octamer or the nucleosome core particle.

Type
Biological Applications of Scanning Probe Microscopies
Information
Microscopy and Microanalysis , Volume 5 , Issue S2: Proceedings: Microscopy & Microanalysis '99, Microscopy Society of America 57th Annual Meeting, Microbeam Analysis Society 33rd Annual Meeting, Portland, Oregon August 1-5, 1999 , August 1999 , pp. 1000 - 1001
Copyright
Copyright © Microscopy Society of America

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References

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