Abstract：
:As visualized by electron microscopy, RecA protein binds in a highly cooperative manner to single-stranded fd DNA in solutions of 0.01 M Tris (pH 7.5). The resulting nucleoprotein filament loops are 1.25 micrometers in length, have a fiber diameter of 12 nm and show an indication of a 4.5 nm repeat along the axis of the compact fibers. RecA binds to linear duplex fd DNA in solutions of 0.01 M Tris (pH 7.5) to yield chains of beads which, in the presence of Mg2+ and ATP, coalesce into smooth filaments with a length of 1.9 micrometers (the length of protein-free fd duplex DNA) and have a fiber diameter of 12 nm. In solutions containing Mg2+ and ATP-gamma-S, however, RecA binds to duplex DNA in a highly cooperative manner to yield rigid filaments 3.0 micrometers in length. These filaments are 12 nm in diameter and show a very clear 7.5 nm axial repeat. This extension of DNA to 150% of its usual length in the apparent absence of any single-stranded components suggests that the DNA helix must also be highly unwound and provides new insights into the mode of RecA action.
journal_name
Celljournal_title
Cellauthors
Dunn K,Chrysogelos S,Griffith Jdoi
10.1016/0092-8674(82)90055-1subject
Has Abstractpub_date
1982-04-01 00:00:00pages
757-65issue
4eissn
0092-8674issn
1097-4172pii
0092-8674(82)90055-1journal_volume
28pub_type
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