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20 years of DNA Polymerase μ, the polymerase that still surprises
Author(s) -
Ghosh Dipayan,
Raghavan Sathees C.
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15852
Subject(s) - dna polymerase , polymerase , biology , dna polymerase mu , primer (cosmetics) , base excision repair , genetics , microbiology and biotechnology , dna replication , dna repair , dna , chemistry , circular bacterial chromosome , organic chemistry
DNA polymerases are important enzymes involved in DNA replication and repair. Based on sequence homology, DNA polymerases have been grouped into distinct families, which are A, B, X, and Y. The Pol X family consists of four members: Pol λ, μ, and β and terminal transferase or TdT. Members of the family X are involved in base excision repair, nonhomologous end joining (NHEJ), and V(D)J recombination. One of the most interesting pol X family members is DNA polymerase μ, discovered back in 2000. Subsequent studies established the importance of Pol μ as a repair polymerase in NHEJ and its interactions with the other proteins of the NHEJ machinery. Pol μ has a number of interesting properties, which sets it apart from the other known DNA polymerases, including its ability to synthesize DNA from an unpaired primer terminus as well in the complete absence of a template strand (terminal transferase activity). Another standout property of Pol μ is its reduced ability to discriminate between ribonucleotides and deoxyribonucleotides and its ability to utilize both ribonucleotides and deoxyribonucleotides as substrates during the gap‐filling stage of NHEJ. In this review, we provide a brief overview of Pol μ in double‐strand break repair and the current knowledge on its various functional aspects.