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. 1984 Jul 11;12(13):5321–5340. doi: 10.1093/nar/12.13.5321

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

A Spassky, S Rimsky, H Garreau, H Buc
PMCID: PMC318922  PMID: 6379600

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.

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