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The RNA polymerase in the Archaea has the same subunits as those present in eukaryotic RNA polymerase II, with the exception that the largest subunit (B prime) has been split into two proteins.

-false
- true

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Final answer:

The statement is false. The Archaea RNA polymerase has the same subunits as eukaryotic RNA polymerase II, except the largest subunit (B prime) is split into two proteins.

Step-by-step explanation:

The statement is false. The RNA polymerase in Archaea has the same subunits as those present in eukaryotic RNA polymerase II, except that the largest subunit (B prime) has been split into two proteins.

In prokaryotes, such as E.coli, the RNA polymerase is composed of five polypeptide subunits: α, α, ß, and ß'. These subunits assemble to form the polymerase core enzyme. The fifth subunit, σ, is involved in transcription initiation. Together, all five subunits form the holoenzyme.

On the other hand, eukaryotic RNA Polymerase II consists of multiple subunits, including Rpb1 (homologous to B prime subunit). However, in Archaea, the B prime subunit is split into two proteins, similar to the prokaryotic RNA polymerase structure.

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