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Skp2 is the substrate recruiting component of the SCFSkp2 complex, which targets cell cycle control elements, such as p27 and p21. [28] [29] [30] Here, SKP2 has been implicated in double negative feedback loops with both p21 and p27, that control cell cycle entry and G1/S transition. [31] [32]
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.
Cdh1 plays a pivotal role in controlling cell division at the end of mitosis and in the subsequent G1 phase of cell cycle: By recognizing and binding proteins (like mitotic cyclins) which contain a destruction box (D-box) and an additional degradation signal (KEN box), Cdh1 recruits them in a C-box-dependent mechanism to the APC for ubiquination and subsequent proteolysis.
Eukaryotic DNA ligase 1 catalyzes a reaction that is chemically universal to all ligases. DNA ligase 1 utilizes adenosine triphosphate (ATP) to catalyze the energetically favorable ligation events in both DNA replication and repair. During the synthesis phase (S-phase) of the eukaryotic cell cycle, DNA replication occurs.
Skp, Cullin, F-box containing complex (or SCF complex) is a multi-protein E3 ubiquitin ligase complex that catalyzes the ubiquitination of proteins destined for 26S proteasomal degradation. [1] Along with the anaphase-promoting complex, [2] SCF has important roles in the ubiquitination of proteins involved in the cell cycle. The SCF complex ...
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 an enzyme that joins together ends of DNA molecules. Although commonly represented as joining two pairs of ends at once, as in the ligation of restriction enzyme fragments, ligase can also join the ends on only one of the two strands (for example, when the other strand is already continuous or lacks a terminal phosphate necessary for ligation).
The discovery of DNA ligase dates back to 1967 and was an important event in the field of molecular biology. [1] Ligation in the laboratory is normally performed using T4 DNA ligase. It is broadly used in vitro due to its capability of joining sticky-ended fragments as well as blunt-ended fragments. [2]