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A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
- T. Paull, E. Rogakou, V. Yamazaki, C. Kirchgessner, M. Gellert, W. Bonner
- Medicine, BiologyCurrent Biology
- 1 August 2000
The evidence presented strongly supports a role for the gamma-H2AX and the PI-3 protein kinase family in focus formation at sites of double-strand breaks and suggests the possibility of a change in chromatin structure accompanying double-Strand break repair.
V(D)J recombination: RAG proteins, repair factors, and regulation.
- M. Gellert
- Biology, MedicineAnnual review of biochemistry
V(D)J recombination is strongly regulated by limiting access to RSS sites within chromatin, so that particular sites are available only in certain cell types and developmental stages, and the roles of enhancers, histone acetylation, and chromatin remodeling factors in controlling accessibility are discussed.
The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks.
This work has investigated the enzymatic activities of the purified proteins and found that Mre11 by itself has 3' to 5' exonuclease activity that is increased when Mre 11 is in a complex with Rad50, which is consistent with the products of nonhomologous end-joining observed in vivo.
Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex.
It is shown that the triple complex of recombinant Nbs1, Mre11, and Rad50 proteins binds cooperatively to DNA and forms a distinct protein-DNA species.
V(D)J recombination: a functional definition of the joining signals.
Although the two signal types share sequence motifs, it is found that there is no evidence of a role in recombination for homology between the signals, suggesting that they serve primarily as protein recognition and binding sites.
Cleavage at a V(D)J recombination signal requires only RAG1 and RAG2 proteins and occurs in two steps
This work shows that purified RAG1 and RAG2 proteins are sufficient to carry out formation of double-strand breaks at recombination signal sequences and makes a hairpin structure at the coding end and a blunt, 5'-phosphorylated signal end.
Helix formation by guanylic acid.
- M. Gellert, M. Lipsett, D. Davies
- Chemistry, MedicineProceedings of the National Academy of Sciences…
- 1 December 1962
From examination of the optical properties of the gel and investigation of the structure of fibers obtained from the gel by drying, it is concluded that, at least in the case of the 5' isomer, the phenomenon may be explained as being due to helix formation by the guanylic acid.
A Stable RAG1–RAG2–DNA Complex That Is Active in V(D)J Cleavage
It is shown that RAG1 and RAG2 bind specifically to this sequence, forming a stable protein-DNA complex, which is able to either nick or form hairpins at the V(D)J signal sequence, depending on the divalent cation present.
Assembly of a 12/23 paired signal complex: a critical control point in V(D)J recombination.
It is shown that all four broken DNA ends remain associated with the RAG proteins in a postcleavage synaptic complex, whose existence helps to explain the known role of RAG1 and RAG2 in the subsequent end-joining events that complete V(D)J recombination.
DNA Transposition by the RAG1 and RAG2 Proteins A Possible Source of Oncogenic Translocations
This RAG-mediated DNA transfer provides strong evidence for the evolution of the V(D)J recombination system from an ancient mobile DNA element and suggests that repeated transposition may have promoted the expansion of the antigen receptor loci.