DNA structural variations in the E. coli tyrT promoter.

Abstract:

:X-ray studies have established that the structure of a right-handed, Watson-Crick double helix can change from place to place along its length as a function of base sequence. The base pairs transmit deformations out to the phosphate backbone, where they can then be recognized by proteins and other DNA-binding reagents. Here we have examined at single-bond resolution the interactions of three commonly used nucleases (DNAase I, DNAase II, and copper-phenanthroline) with a DNA of natural origin, the 160 bp tyrT promoter. All three of these reagents seem sensitive to DNA backbone geometry rather than base sequence per se. Their sequence-dependent patterns of cleavage provide evidence for structural polymorphism of several sorts: global variation in helix groove width, global variation in radial asymmetry, and local variation in phosphate accessibility. These findings explain how sequence zones of a certain base composition, or purine-pyrimidine asymmetry, can influence the recognition of DNA by protein molecules.

journal_name

Cell

journal_title

Cell

authors

Drew HR,Travers AA

doi

10.1016/0092-8674(84)90379-9

subject

Has Abstract

pub_date

1984-06-01 00:00:00

pages

491-502

issue

2

eissn

0092-8674

issn

1097-4172

pii

0092-8674(84)90379-9

journal_volume

37

pub_type

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