E.coli MukB protein involved in chromosome partition forms a homodimer with a rod-and-hinge structure having DNA binding and ATP/GTP binding activities.

作者: H. Niki , R. Imamura , M. Kitaoka , K. Yamanaka , T. Ogura

DOI: 10.1002/J.1460-2075.1992.TB05617.X

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摘要: Abstract mukB mutants of Escherichia coli are defective in the correct partitioning replicated chromosomes. This results appearance normal-sized anucleate (chromosome-less) cells during cell proliferation. Based on nucleotide sequence mukB gene, MukB protein 177 kDa was predicted to be a filamentous with globular domains at ends, and also having DNA binding abilities. Here we present evidence that purified possesses these characteristics. forms homodimer rod-and-hinge structure pair large, C-terminal one end small, N-terminal opposite end; it tends bend middle hinge site rod section. Chromatography DNA-cellulose column gel retardation assay revealed activity. Photoaffinity cross-linking experiments showed binds ATP GTP presence Zn2+. Throughout purification steps, acyl carrier co-purified MukB.

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