Spiral structure of Escherichia coli HUalphabeta provides foundation for DNA supercoiling.

Abstract:

:We determined the crystal structure of the Escherichia coli nucleoid-associated HUalphabeta protein by x-ray diffraction and observed that the heterodimers form multimers with octameric units in three potential arrangements, which may serve specialized roles in different DNA transaction reactions. It is of special importance that one of the structures forms spiral filaments with left-handed rotations. A negatively superhelical DNA can be modeled to wrap around this left-handed HUalphabeta multimer. Whereas the wild-type HU generated negative DNA supercoiling in vitro, an engineered heterodimer with an altered amino acid residue critical for the formation of the left-handed spiral protein in the crystal was defective in the process, thus providing the structural explanation for the classical property of HU to restrain negative supercoils in DNA.

authors

Guo F,Adhya S

doi

10.1073/pnas.0611686104

subject

Has Abstract

pub_date

2007-03-13 00:00:00

pages

4309-14

issue

11

eissn

0027-8424

issn

1091-6490

pii

0611686104

journal_volume

104

pub_type

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