H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro.

Abstract:

:We characterize a component of the E. coli bacterial nucleoid H1a, which accumulates in stationary phase. This protein, identical with the major component of a plasmid-protein complex previously isolated in our laboratory, has a pI close to 7.5. Acrylamide gel electrophoresis and sedimentation in sucrose gradient have shown that the protein H1a induces significant compaction into DNA. This compaction is equivalent to that observed in nucleosome core although it introduces only a slight change in linking number. In addition, the structural change induced in the lactose L8UV5 promoter by H1a results in the decrease in the kinetic of formation of the open complex with RNA polymerase.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Spassky A,Rimsky S,Garreau H,Buc H

doi

10.1093/nar/12.13.5321

subject

Has Abstract

pub_date

1984-07-11 00:00:00

pages

5321-40

issue

13

eissn

0305-1048

issn

1362-4962

journal_volume

12

pub_type

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