Open AccessEukaryotic TLS polymerases
Author(s) -
Przemysław Piotr Tomczyk,
Ewelina Synowiec,
Daniel Wysokiński,
Katarzyna Woźniak
Publication year - 2016
Publication title -
postępy higieny i medycyny doświadczalnej
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.275
H-Index - 34
eISSN - 1732-2693
pISSN - 0032-5449
DOI - 10.5604/17322693.1202481
Subject(s) - polymerase , dna polymerase , biology , sumo protein , microbiology and biotechnology , dna replication , dna damage , genetics , dna clamp , ubiquitin , computational biology , dna , polymerase chain reaction , reverse transcriptase , gene
TLS polymerases are able to replicate damaged DNA (called translesion DNA synthesis, TLS). Their presence prevents cell death as a result of violating the integrity of the genome. In vitro, they are mutator, but in vivo are recruited by specific types of DNA damage and usually replicate them in a correct manner. The best-known TLS polymerases belong to the Y family, such as Rev1, κ, η, ι, and polymerase ζ from the B family. There are two mechanisms of TLS polymerases action: polymerase-switching model and the gap-filling model. Selection of the mechanism primarily depends on the phase of the cell cycle. The regulation of these polymerases may take place at the transcriptional level and at level of recruitment to the sites of DNA damage. In the latter case post-translational modification of proteins - ubiquitination and sumoylation, and protein-protein interactions are crucial.