DNA polymerase and RNA polymerase (No universal single abbreviation; commonly as "DNAP" (for DNA polymerase) and "RNAP" (for RNA polymerase) in the literature.)

DNA polymerases are essential enzymes that synthesize new DNA strands using existing DNA as templates during replication and repair, acting in processes vital for genome maintenance, fidelity, and transmission. RNA polymerases are large multi-subunit enzyme complexes that transcribe DNA into RNA, a central step in gene expression. Both polymerases are classified as nucleotidyltransferases but differ in substrate specificity, cofactor requirements, and biological context. DNA polymerases require primers and catalyze DNA synthesis, while RNA polymerases initiate RNA chains without primers and perform unwinding of DNA during transcription. Both families are of major biomedical importance, as they are critical to cell proliferation, genomic integrity, and are prime therapeutic targets in cancer, infectious diseases, and genetic disorders. Targeting these enzymes underlies the mechanism of a broad spectrum of drugs including antivirals, antibiotics, and anticancer agents.

Other names

DNA-directed DNA polymeraseDNA replicaseRNA-directed RNA polymerase (for viral variants)DNA-directed RNA polymeraseTranscriptaseDNA pol (for DNA polymerase)RNA pol (for RNA polymerase)Human subtypes: POLA1 (DNA polymerase alpha), POLB, etc.; POLR2A (RNA polymerase II catalytic subunit), and others

Inhibition of nucleotide incorporation (competitive analogs) Chain termination (nucleoside/nucleotide analogs prevent elongation) Enzyme active site binding/blocking Conformational change or subunit dissociation inhibition