The process whereby new strands of DNA are synthesized in the mitochondrion.

The process by which a transformation is induced in the tertiary structure of a DNA helix. This may be mediated by helicases, which can unwind the DNA duplex, thereby inducing formation of supercoils, or topoisomerases, which catalyze addition or removal of supercoils.

The re-formation of a broken phosphodiester bond in the DNA backbone, carried out by DNA ligase.

pre-replicative complex formation and maintenance

The assembly and maintenance of the pre-replicative complex, multiprotein complex that forms at eukaryotic DNA replication origins during late M phase; its presence is required for replication initiation.

The process by which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating unpaired template strands for DNA replication.

DNA replication, synthesis of RNA primer

The generation, by DNA polymerase alpha, of an RNA primer followed by a short segment of DNA on the lagging strand of the replicating DNA.

The breakdown into simpler components of UDP, uridine (5'-)diphosphate.

aminoacyl-tRNA synthetase auxiliary protein activity

A multienzyme complex found in all multicellular eukaryotes composed of eight proteins with aminoacyl-tRNA synthetase activities (abbreviated as: ArgRS, AspRS, GluProRS, GlnRS, IleRS, LeuRS, LysRS, MetRS where RS is the enzyme, preceded by the amino acid it uses as a substrate) as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. Several of these subunits are known dimers, so the total polypeptide count in the multisynthetase complex is at least fifteen. All of the enzymes in this assembly catalyze the same reaction, the covalent attachment of an amino acid to either the 2'- or 3'-hydroxyl of the 3'-terminal adenosine of tRNA, but using different substrates.

methionyl glutamyl tRNA synthetase complex

A complex consisting of methionyl- and glutamyl-tRNA synthetases. The tRNA synthetases present in the complex bind to their cognate tRNAs more efficiently than they do as monomers.