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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).
S phase (Synthesis phase) is the phase of the cell cycle in which DNA is replicated, occurring between G 1 phase and G 2 phase. [1] Since accurate duplication of the genome is critical to successful cell division, the processes that occur during S-phase are tightly regulated and widely conserved.
During adenylylation, there is a nucleophilic attack on the alpha phosphate of ATP from a catalytic lysine resulting in the production of inorganic pyrophosphate (PPi) and a covalently bound lysine-AMP intermediate in the active site of DNA ligase 1. During the AMP transfer step, the DNA ligase becomes associated with the DNA, locates a nick ...
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.
The mechanism of the ligation reaction was first elucidated in the laboratory of I. Robert Lehman. [4] [5] Two fragments of DNA may be joined by DNA ligase which catalyzes the formation of a phosphodiester bond between the 3'-hydroxyl group (-OH) at one end of a strand of DNA and the 5'-phosphate group (-PO4) of another.
The eukaryotic cell cycle consists of four distinct phases: G 1 phase, S phase (synthesis), G 2 phase (collectively known as interphase) and M phase (mitosis and cytokinesis). M phase is itself composed of two tightly coupled processes: mitosis, in which the cell's nucleus divides, and cytokinesis, in which the cell's cytoplasm and cell membrane divides forming two daughter cells.
Next, biochemical studies revealed that Cdc34 is an E2 enzyme that physically interacts with an E3 ubiquitin ligase complex containing Skp1, Cdc4, and several other proteins. [6] Skp1’s known binding partners—specifically Skp2, Cyclin F, and Cdc4—were found to share an approximately 40 residue motif that was coined the F-box motif.
HERC2 is a giant E3 ubiquitin protein ligase, implicated in DNA repair regulation, pigmentation and neurological disorders.It is encoded by a gene of the same name belonging to the HERC family, which typically encodes large protein products with C-terminal HECT domains and one or more RCC1-like (RLD) domains.