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Formation of a RNA polymerase sub-assembly composed of subunit alpha from Escherichia coli and of subunit beta from Micrococcus luteus.

Authors
  • Lill, U I
  • Hartmann, G R
Type
Published Article
Journal
Hoppe-Seyler's Zeitschrift fur physiologische Chemie
Publication Date
Dec 01, 1977
Volume
358
Issue
12
Pages
1605–1608
Identifiers
PMID: 338461
Source
Medline
Language
English
License
Unknown

Abstract

Functionally equivalent subunits of RNA polymerase from Micrococcus luteus and Escherichia coli differ from each other in many molecular and antigenic properties. In spite of these differences, subunit alpha from E. coli and subunit beta from M. luteus form a complex alpha2beta, when incubated together. This complex binds rifampicin tightly, which the isolated subunits do not. The hybrid complex is very similar in its properties to the complex alpha2beta formed only from E. coli or M. luteus subunits. Since the sub-assembly alpha2beta from E. coli is reported to be an obligatory intermediate in the assembly process of complete RNA polymerase, the newly described hybrid sub-assembly may function similarly as an intermediate in the formation of the hybrid form of RNA polymerase described earlier.

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