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HU and IHF, two homologous histone‐like proteins of Escherichia coli, form different protein‐DNA complexes with short DNA fragments.
Author(s) -
Bonnefoy E.,
RouvièreYaniv J.
Publication year - 1991
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1991.tb07998.x
Subject(s) - dna , escherichia coli , biology , microbiology and biotechnology , histone , biochemistry , gene
Using the gel retardation technique we have studied the protein‐DNA complexes formed between HU–the major histone‐like protein of Escherichia coli–and short DNA fragments. We show that several HU heterodimers bind DNA in a regularly spaced fashion with each heterodimer occupying about 9 base pairs. The alpha 2 and beta 2 HU homodimers form the same structure as the alpha beta heterodimer on double stranded DNA. However when compared to the heterodimer, they bind single stranded DNA with higher affinity. We also show that HU and the Integration Host Factor of E. coli (IHF) form different structures with the same DNA fragments. Moreover, HU seems to enhance the DNA‐binding capacity of IHF to a DNA fragment which does not contain its consensus sequence.