Mechanism of DNA compaction by yeast mitochondrial protein Abf2p.

Abstract:

:We used high-resolution atomic force microscopy to image the compaction of linear and circular DNA by the yeast mitochondrial protein Abf2p, which plays a major role in packaging mitochondrial DNA. Atomic force microscopy images show that protein binding induces drastic bends in the DNA backbone for both linear and circular DNA. At a high concentration of Abf2p DNA collapses into a tight nucleoprotein complex. We quantified the compaction of linear DNA by measuring the end-to-end distance of the DNA molecule at increasing concentrations of Abf2p. We also derived a polymer statistical mechanics model that provides a quantitative description of compaction observed in our experiments. This model shows that sharp bends in the DNA backbone are often sufficient to cause DNA compaction. Comparison of our model with the experimental data showed excellent quantitative correlation and allowed us to determine binding characteristics for Abf2p. These studies indicate that Abf2p compacts DNA through a simple mechanism that involves bending of the DNA backbone. We discuss the implications of such a mechanism for mitochondrial DNA maintenance and organization.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Friddle RW,Klare JE,Martin SS,Corzett M,Balhorn R,Baldwin EP,Baskin RJ,Noy A

doi

10.1016/S0006-3495(04)74231-9

subject

Has Abstract

pub_date

2004-03-01 00:00:00

pages

1632-9

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(04)74231-9

journal_volume

86

pub_type

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