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Volume 271, Number 44, Issue of November 1, 1996 pp. 27969-27974
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Structural Modules of the Large Subunits of RNA Polymerase
INTRODUCING ARCHAEBACTERIAL AND CHLOROPLAST SPLIT SITES IN THE beta  AND beta ' SUBUNITS OF ESCHERICHIA COLI RNA POLYMERASE

(Received for publication, April 27, 1996, and in revised form, July 24, 1996)

Konstantin Severinov Dagger , Arkady Mustaev , Aleksandr Kukarin par , Oriana Muzzin Dagger , Irina Bass par , Seth A. Darst Dagger and Alex Goldfarb

From Dagger  The Rockefeller University, New York, New York 10021, the  Public Health Research Institute, New York, New York 10016, and the par  Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, Russia 123182

The beta  and beta ' subunits of Escherichia coli DNA-dependent RNA polymerase are highly conserved throughout eubacterial and eukaryotic kingdoms. However, in some archaebacteria and chloroplasts, the corresponding sequences are ``split'' into smaller polypeptides that are encoded by separate genes. To test if such split sites can be accommodated into E. coli RNA polymerase, subunit fragments encoded by the segments of E. coli rpoB and rpoC genes corresponding to archaebacterial and chloroplast split subunits were individually overexpressed. The purified fragments, when mixed in vitro with complementing intact RNA polymerase subunits, yielded an active enzyme capable of catalyzing the phosphodiester bond formation. Thus, the large subunits of eubacteria and eukaryotes are composed of independent structural modules corresponding to the smaller subunits of archaebacteria and chloroplasts.


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