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In biochemistry, a ligase is an enzyme that can catalyze the joining of two molecules by forming a new chemical bond.This is typically via hydrolysis of a small pendant chemical group on one of the molecules, typically resulting in the formation of new C-O, C-S, or C-N bonds.
DNA ligase is a type of enzyme that facilitates the joining of DNA strands together by catalyzing the formation of a phosphodiester bond.It plays a role in repairing single-strand breaks in duplex DNA in living organisms, but some forms (such as DNA ligase IV) may specifically repair double-strand breaks (i.e. a break in both complementary strands of DNA).
The smallest known eukaryotic ligase is Chlorella virus DNA ligase (ChVLig). It contains only 298 amino acids. When ChVLig is the only source of ligase in the cell, it can continue to support mitotic development, and nonhomologous end joining in budding yeasts. [34] DNA Ligase I (Lig1) is accountable for Okazaki Fragments ligation.
Ligase I has also been found to be upregulated in proliferating tumor cells, as opposed to benign tumor cell lines and normal human cells. Furthermore, it has been shown that inhibiting ligase I expression in these cells can have a cytotoxic effect, suggesting that ligase I inhibitors may be viable chemotherapeutic agents.
The repair mechanisms of these sites are not fully revealed. The NHEJ is the dominant DNA repair pathway throughout the cell cycle. The DNA-PKcs protein is the critical element in the center of NHEJ. Using DNA-PKcs KO cell lines or inhibition of DNA-PKcs does not affect the repair capacity of HLS.
3980 16882 Ensembl ENSG00000005156 ENSMUSG00000020697 UniProt P49916 P97386 RefSeq (mRNA) NM_002311 NM_013975 NM_001291245 NM_001291246 NM_001291247 NM_010716 RefSeq (protein) NP_002302 NP_039269 n/a Location (UCSC) Chr 17: 34.98 – 35.01 Mb Chr 11: 82.67 – 82.7 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse DNA ligase 3 also DNA ligase III, is an enzyme that, in humans, is ...
Pathway preference may differ between organisms, as well. While human cells utilize both short- and long-patch BER, the yeast Saccharomyces cerevisiae was long thought to lack a short-patch pathway because it does not have homologs of several mammalian short-patch proteins, including pol β, DNA ligase III, XRCC1, and the kinase domain of PNKP.
Glutamate cysteine ligase modifier subunit (GCLM, ~31 kDa) has no enzymatic activity on its own but increases the catalytic efficiency of GCLC when complexed in the holoenzyme. In the majority of cells and tissues, the expression of GCLM protein is lower than GCLC and GCLM is therefore limiting in the formation of the holoenzyme complex.