(Converted)-5 - Journal of Cell and Molecular Biology - Haliç ...
(Converted)-5 - Journal of Cell and Molecular Biology - Haliç ...
(Converted)-5 - Journal of Cell and Molecular Biology - Haliç ...
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core <strong>and</strong> holoenzyme (Burgess, 1969). The omega<br />
subunit was for many years considered a curiosity<br />
since no function could be ascribed to it. Therefore, the<br />
available literature on the ω subunit as regards to its<br />
structure <strong>and</strong> function is rare. The ω subunit is not<br />
required for the function <strong>of</strong> the transcriptional<br />
apparatus both in vivo <strong>and</strong> in vitro. Strain lacking ω,<br />
that is, a rpoZ null mutant is viable, suggesting a nonessential<br />
nature <strong>of</strong> the protein or that there might also<br />
be a redundancy in function. The only known<br />
phenotype ascribed to the rpoZ null mutant is a slower<br />
growth time (Mukherjee et al., 1999). However, it is<br />
now known that omega is necessary to restore<br />
denatured RNA polymerase in vitro to its fully<br />
functional form. It may function by binding<br />
simultaneously to the N-terminus <strong>and</strong> C-terminus <strong>of</strong><br />
the β' subunit. The omega subunit is a part <strong>of</strong> the<br />
Thermus aquaticus enzyme whose structure was<br />
recently determined (Murakami et al., 2002).<br />
A study by Mukharjee <strong>and</strong> Chatterji (1999) showed<br />
that ω-less holoenzyme has lesser affinity towards the<br />
DNA template <strong>and</strong> external addition <strong>of</strong> ω destabilizes<br />
the open complex for both the wild-type <strong>and</strong> ω-less<br />
enzyme. The ω-less core enzyme interacts with the σ 70<br />
subunit to expose the –35 recognition domain (domain<br />
4·2) unlike that observed in the wild-type interaction.<br />
Thus the absence <strong>of</strong> the ω subunit leads to the<br />
formation <strong>of</strong> an enzyme which has altered DNA<br />
binding <strong>and</strong> σ 70 binding properties. Circular dichroic<br />
measurements also indicate a major conformational<br />
alteration <strong>of</strong> both holo <strong>and</strong> core RNA polymerase in<br />
the presence <strong>and</strong> absence <strong>of</strong> the ω subunit.<br />
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