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Primary structure of Escherichia coli RNA polymerase nucleotide substitution in the β subunit gene of the rifampicin resistant rpoB255 mutant

✍ Scribed by Ovchinnikov, Yu. A. ;Monastyrskaya, G. S. ;Gubanov, V. V. ;Lipkin, V. M. ;Sverdlov, E. D. ;Kiver, I. F. ;Bass, I. A. ;Mindlin, S. Z. ;Danilevskaya, O. N. ;Khesin, R. B.


Publisher
Springer
Year
1981
Tongue
English
Weight
609 KB
Volume
184
Category
Article
ISSN
0026-8925

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✦ Synopsis


The transducing phage 2 dsupM814 and the plasmid rpIK A l L rpo 8 plB1830 containing the wild-type rpoB gene have been constructed and the primary structure °f the gene's central fragment l l l has been established. In contrast with the wild-type, the gene g G C of the rpoB255 mutant, whose primary structure has been pub-~ lished, was found to contain an A.T.~T.A. transversion entailing the substitution of a valine residue for the aspartic acid residue (516) of the wild-type/3 subunit. rpo C ot Fig. 1. Restriction map of E. coli DNA within the rpoB gene. The sites for restriction endonucleases EeoRI (4,) and PstI (z~) are shown


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