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Isopentenyl diphosphate isomerase (IPI) is a core enzyme in isoprenoid biosynthesis (Ramos-Valdivia et al. 1997).
In phagocytes, two transmembrane proteins (gp91phox and p22phox) interact with each other to form a stable core enzyme, flavocytochrome b558.
We previously showed that the toroidal structure could be split off from the core enzyme of Thermotoga maritima topoisomerase I by limited proteolysis.
Binding of the core enzyme, consists of the five core subunits—β´, β, a dimer of identical α subunits, and the ω subunit.
PP-2A exists in both core enzyme and holoenzyme within cells [6] [7].
As seen from Figure 6A, the initial rates of RNA synthesis by the core enzyme were boosted at higher core enzyme concentrations (Figure 6A) due to the possible 'dimerization' of RNA polymerase.
The dimeric PP2A core enzyme consists of a catalytic C subunit (PP2Ac) and a structural A subunit.
To perform the reaction, E. coli RNA polymerase core enzyme was reconstituted with purified his-tagged RpoD from S. mutans.
We next sought to study how self-association of the RNA polymerase core enzyme might affect its transcriptional activity.
We demonstrated before, that no single round transcription takes place with core enzyme alone (data not shown).
Likewise, these experiments showed no detectable radioactivity co-migrating with the core enzyme in gel-filtration (data not shown).
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