Rad50 [13B3]

13B3

Amino acids 1-425 of Rad50 expressed in E. coli.

Rad50

1 mg/ml

Phosphate-buffered saline pH 7. 4 containing no preservatives

153 Cellular

Component of the MRN complex which plays a central role in double-strand break (DSB) repair DNA recombination maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3\' -5\' exonuclease activity which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11A to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation. Cofactor: Binds 1 zinc ion per homodimer (By similarity).

Nucleus. Telomere. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents.

The zinc-hook which separates the large intramolecular coiled coil regions contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule thereby forming a V-shaped homodimer. The two heads of the homodimer which constitute the ATP-binding domain interact with the MRE11A homodimer (By similarity).

In case of infection by adenovirus E4 the MRN complex is inactivated and degraded by viral oncoproteins thereby preventing concatenation of viral genomes in infected cells.

Contains 1 zinc-hook domain.