Subunit assembly and metabolic stability ofE. coliRNA polymerase
作者:
Akira Ishihama,
Nobuyuki Fujita,
Robert E. Glass,
期刊:
Proteins: Structure, Function, and Bioinformatics
(WILEY Available online 1987)
卷期:
Volume 2,
issue 1
页码: 42-53
ISSN:0887-3585
年代: 1987
DOI:10.1002/prot.340020106
出版商: Wiley Subscription Services, Inc., A Wiley Company
关键词: proteolytic cleavage;immunological cross‐reaction;amber fragment;temperature‐sensitive mutant;stationary growth‐phase
数据来源: WILEY
摘要:
AbstractImmunological cross‐reaction was employed for identification of proteolytic fragments ofE. coliRNA polymerase genered both in vitro and in vivo. Several species of partially denatured but assembled RNA polymerase were isolated, which were composed of fragments of the two large subunits, β and β′, and the two small and intact subunits, α and σ. Comparison of the rate and pathway of proteolytic cleavage in vitro of unassembled subunits, subassemblies, and intact enzymes indicated that the susceptibility of RNA polymerase subunits to proteolytic degradation was dependent on the assembly state.Using this method, degradation in vivo was found for some, but not all, of the amber fragments of β subunit in merodiploid cells carrying both wild‐type and mutantrpoBgenes. Although the RNA polymerase is a metabolically stable component in exponentially growing cells ofE. coli, degradation of the full‐sized subunits was found in two cases, i.e., several temperature‐sensitiveE. colimutants with a defect in the assembly of RNA polymerase and the stationary‐phase cells of a wild‐typeE. coli. The in vivo degradation of RNA polymerase was indicated to be initiated by alteration of th
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