DNA binding and bending by a chloroplast-encoded HU-like protein overexpressed in Escherichia coli.
The Guillardia theta chloroplast hlpA gene encodes a protein resembling bacterial histone-like protein HU. This gene was cloned and overexpressed in Escherichia coli cells, and the resulting protein product, HlpA, was purified and characterized in vitro. In addition to exhibiting a general DNA-binding activity, the chloroplast HlpA protein also strongly facilitated cyclization of a short DNA fragment in the presence of T4 DNA ligase, indicating its ability to mediate very tight DNA curvatures.
Wu
H
H
Biochemistry Department, Dalhousie University, Halifax, Nova Scotia, Canada.
Liu
X Q
XQ
D001426:Bacterial Proteins / Q000235:genetics*; D002736:Chloroplasts / Q000737:chemistry* / Q000235:genetics*; D004268:DNA-Binding Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D056890:Eukaryota / Q000235:genetics*; D019143:Evolution, Molecular; D010940:Plant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C106634:HLPA protein, Guillardia theta; D010940:Plant Proteins; C040330:histone-like protein HU, bacteria