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The process of V(D)J recombination is mediated by VDJ recombinase, which is a diverse collection of enzymes. The key enzymes involved are recombination activating genes 1 and 2 (RAG), terminal deoxynucleotidyl transferase (TdT), and Artemis nuclease, a member of the ubiquitous non-homologous end joining (NHEJ) pathway for DNA repair. [4]
The Artemis complex is a protein complex that functions in V(D)J recombination, the somatic recombination process which generates diversity in T cell receptors and immunoglobulins. Mutations in the Artemis complex results in hypersensitivity to DNA double-strand break-inducing agents, such as radiation; and so people with mutations in the ...
Current studies have indicated that RAG-1 and RAG-2 must work in a synergistic manner to activate VDJ recombination. RAG-1 was shown to inefficiently induce recombination activity of the VDJ genes when isolated and transfected into fibroblast samples. When RAG-1 was cotransfected with RAG-2, recombination frequency increased by a 1000-fold. [3]
Generation of junctional diversity through recombination illustrated between two gene segments: D (blue) and J (green). Sections highlighted in red show nucleotides added at each stage. Junctional diversity describes the DNA sequence variations introduced by the improper joining of gene segments during the process of V(D)J recombination.
Recombination signal sequences guide the enzyme complex to the V, D, and J gene segments that will undergo recombination during the formation of the heavy and light-chain variable regions in T-cell receptors and immunoglobulin molecules. [1]
Susumu Tonegawa (利根川 進, Tonegawa Susumu, born September 5, 1939) is a Japanese scientist who was the sole recipient of the Nobel Prize for Physiology or Medicine in 1987 for his discovery of V(D)J recombination, the genetic mechanism which produces antibody diversity. [1]
The 2-15nt DNA fragments produced in vivo are hypothesized to act in signaling pathways related to DNA repair and/or recombination machinery. [13] Like many polymerases, TdT requires a divalent cation cofactor , [ 15 ] however, TdT is unique in its ability to use a broader range of cations such as Mg 2+ , Mn 2+ , Zn 2+ and Co 2+ . [ 15 ]
This causes different recombination hybrid sites to be reconstituted in the recombination products. Joining of left ends to left or right to right is avoided due to the asymmetric "overlap" sequence between the staggered points of top and bottom strand exchange, which is in stark contrast to the mechanism employed by tyrosine recombinases.