Search results
Results from the WOW.Com Content Network
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).
27401 Ensembl ENSG00000145604 ENSMUSG00000054115 UniProt Q13309 Q9Z0Z3 RefSeq (mRNA) NM_001243120 NM_005983 NM_032637 NM_001285980 NM_013787 NM_145468 RefSeq (protein) NP_001230049 NP_005974 NP_116026 NP_001272909 NP_038815 Location (UCSC) Chr 5: 36.15 – 36.2 Mb Chr 15: 9.11 – 9.16 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse S-phase kinase-associated protein 2 is an enzyme ...
After binding of a target protein to the F-box protein, the ubiquitin is transferred from E2 and attached via a peptide bond to a lysine side chain in the target protein. (b) A composite model structure for human SCF derived from X-ray structures of human Rbx1–Cul1–Skp1–Skp2 complex and the E2 enzyme Ubc7.
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.
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 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]
During G1 phase, the two head-to-head Mcm2-7 rings serve as the scaffold for the assembly of the bidirectional replication initiation complexes at the replication origin. During S phase, the Mcm2-7 complex forms the catalytic core of the Cdc45-MCM-GINS helicase - the DNA unwinding engine of the replisome.
The G1/S cell cycle checkpoint controls the passage of eukaryotic cells from the first gap phase, G1, into the DNA synthesis phase, S. In this switch in mammalian cells, there are two cell cycle kinases that help to control the checkpoint: cell cycle kinases CDK4/6-cyclin D and CDK2-cyclin E. [ 1 ] The transcription complex that includes Rb and ...