Interaction of the Escherichia coli HU protein with DNA.
Isolation and characterization of gene 5 protein of filamentous bacterial viruses. Links to PubMed are also available for Selected References. Get a printable copy (PDF file) of the complete article (3.0M), or click on a page image below to browse page by page. Full textįull text is available as a scanned copy of the original print version. Nucleoprotein formed with single-stranded ΦX174 DNA had a diameter of ∼11 nm and could form circles with a contour length of 0.5 μm. Both structures showed no significant contraction of the length of the DNA covered in the complex. At higher protein concentration than needed to package all DNA into the complex with two double-stranded DNAs, the two DNAs were separated again and a new structure was formed evenly covering only one DNA strand. The complex consists of two right-handed, interwound fibers, with a helical pitch of 26 nm and a diameter of ∼10-11 nm. Using double-stranded DNA, 10b first bound cooperatively to two strands forming long, plait-like structures only slightly shorter than respective free DNA. Protein 10b showed three different types of regular structures: one with single-stranded and two with double-stranded DNA. Protein 10a, at low protein concentrations, showed individual small spots on the DNA and at high concentrations evenly covered doublestranded DNA. Two of the proteins (10a and 10b) formed specific structures after incubation with DNA.
DNA-protein complexes formed in vitro with isolated DNA-binding proteins from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius were analyzed by electron microscopy.
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