RNA-dependent DNA polymerase

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RNA-dependent DNA polymerase is an enzyme that catalyzes the transcription of RNA into DNA. This process is crucial for the replication of retroviruses, including the well-known Human Immunodeficiency Virus (HIV). The enzyme is more commonly referred to as reverse transcriptase.

Function[edit | edit source]

RNA-dependent DNA polymerase synthesizes a complementary DNA strand from an RNA template. This is the reverse of the usual transcription process, where DNA serves as a template for RNA synthesis. The enzyme's activity is a key step in the retroviral replication cycle, allowing the viral RNA genome to be integrated into the host's DNA, thereby enabling the virus to replicate within the host cell.

Structure[edit | edit source]

The enzyme typically consists of several subunits, which include domains responsible for its polymerase activity as well as an RNase H domain. The RNase H domain is crucial for removing the RNA template after the synthesis of the complementary DNA strand.

Clinical Significance[edit | edit source]

The ability of RNA-dependent DNA polymerase to reverse-transcribe viral RNA into DNA makes it a prime target for antiretroviral drugs, particularly in the treatment of HIV/AIDS. Inhibitors of the enzyme, such as nucleoside reverse transcriptase inhibitors (NRTIs) and non-nucleoside reverse transcriptase inhibitors (NNRTIs), are key components of antiretroviral therapy, significantly reducing the viral load in patients.

Research and Development[edit | edit source]

Ongoing research aims to improve the efficacy and reduce the side effects of reverse transcriptase inhibitors. Additionally, understanding the structure and function of RNA-dependent DNA polymerase at a molecular level is crucial for the development of new therapeutic strategies against retroviruses.


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Contributors: Prab R. Tumpati, MD