Skip to main content
. 2020 May 22;8:e9197. doi: 10.7717/peerj.9197

Table 1. Summary of the most damaging effects of Rad50 mutations obtained from previous in vitro and in vivo experiments.

Motif/domain Mutations Organism Effects References
Walker A K40A/R/E S. cerevisiae • HR and NHEJ defects and lower ATPase activity Chen et al. (2005)
Walker A D-loop N38A, D512N/A T4 bacteriophage • Naturally occurring mutation of CFTR protein De La Rosa & Nelson (2011)
• Reduce in ATP activity
ATP binding domain and Walker A G39D, K40E, K81I, R20M S. cerevisiae • Total defect in formation of viable spore Alani, Padmore & Kleckner (1990)
ATP binding domain K6E, K22M, R83I M. musculus • Embryonic lethality, growth defect, cancer predisposition, hematopoietic and spermatogenic depletion Bender et al. (2002)
Walker A K39R, K42M D. radiodurans • Prevented ATP binding and hydrolysis Koroleva et al. (2007)
ATPase binding domain, Walker B and Signature motif K115E, K175E, K182E, R94E, K95E, R765E T. maritima In vitro: Thermotoga maritima Rojowska et al. (2014)
• K175E, K182E, K115E Reduced DNA binding
• R94E and K95E: Important for DNA binding
• R765E: Diminished DNA binding
• E798Q: Low affinity to DNA
• S768R: Reduced DNA binding
E798Q, S768R, K103E, K104E, R131E, R1202E, S1205R, E1235Q S. cerevisiae In vivo: Saccharomyces cerevisiae
• S1205R and E1235Q double mutation: Unable to rescue the impaired DNA damage response
• K103E, K104E and R131E: Strongly affected DNA binding and moderate reduction in telomere length
• K103E and R131R (double mutation) and R1201E: Significantly reduced telomere length
• S1205R: Significantly reduced telomere length
Zinc hook S679R, P682E, V683R M. musculus • Lethality in mice. Hydrocephalus, defects in primitive hematopoietic and gametogenic cells Roset et al. (2014)
C684N, C685A, P686A, V6871, C688R, Q689S S. cerevisiae • Defective to be recruited to chromosomal double strand break He et al. (2012)
• Phenotype as severe as Rad50 null mutant
• Defective in ATM activation, HR, sensitive to irradiation and ATR activation
C288S, C291S T4 bacteriophage • Double mutation is lethal Barfoot et al. (2015)
S635G H. sapiens • Chromosomal instability Gatei et al. (2011)
• Defective ATM-dependent signaling
S685R, Y688E, L689R S. cerevisiae • S685R and Y688E double mutation: Sporulation efficiency and viability were severely impaired followed by L689R Hohl et al. (2015)
• Rad50-Mre11 interaction was strongly impaired, partial suppression of telomere and meiotic defects
Rad50 Signature motif R805E, L802W P. furiosus • L802W: Decrease dimerization in ATP, hydrolysis and cleavage site Deshpande et al. (2014)
• R805E: Poorly grown in camptothecin; inability to repair endogenous DNA damage by HR and showed defect in resection in HO endonuclease induced
K1187A, K1187E, R1195A, R1195E S. pombe • K1187A: Sensitive in higher dose of clastogens Williams et al. (2011)
• K1187E, R1195A and R1195E: Significantly sensitive to clastogen agents and were deleterious as Rad50 null mutation
S471A/R/M, E474Q, K475M T4 bacteriophage • S471A/R.M, E474Q and K475M: Residues involved in the allosteric transmission between DNA and ATP binding sites Herdendorf & Nelson (2011)
S1205R S. cerevisiae • S1202R: Reduced adenylate kinase Bhaskara et al. (2007)
S793R P. furiosus • S793R: Deficient in ATP-dependent dimer formation and ATP binding
S1202R H. sapiens • S1202R and S1205R: Low level of adenylate kinase
• S1205R: Telomere shortening, not support spore viability
Signature motif and Q loop S793R, Q140H P. furiosus • S793R: Analogs to the mutation in CFTR (S549R) gene that results cystic fibrosis Moncalian et al. (2004)
• S793R: Prevented ATP binding
S1205R S. cerevisiae • S1205R S. cerevisiae: Failed to complement Rad50 deletion strain in DNA repair assay
• S783R and Q140H: Halted ATP-dependent activities
ATPase domain R1093 (stop) c.3939A/T H. sapiens • Nijmegen breakage syndrome like disorder (NBSLD) Waltes et al. (2009)

Note:

HR, homologous recombination; NHEJ, non-homologous end joining repair; CFTR, cystic fibrosis transmembrane conductance regulator; ATP, adenosine tri-phosphate; ATM, ataxia-telangiectasia mutated; ATR, ATM-and Rad3-Related. Refer to Table S2 for the description of all mutations.