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Literature summary for 2.1.1.360 extracted from

  • Lazzaro, F.; Sapountzi, V.; Granata, M.; Pellicioli, A.; Vaze, M.; Haber, J.E.; Plevani, P.; Lydall, D.; Muzi-Falconi, M.
    Histone methyltransferase Dot1 and Rad9 inhibit single-stranded DNA accumulation at DSBs and uncapped telomeres (2008), EMBO J., 27, 1502-1512.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
Y798Q the point mutation within the Tudor domain prevents Rad9 binding to chromatin and Rad9 hyperphosphorylation after DNA damage Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + histone H3(K79)
-
 Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
Dot1
-
 Saccharomyces cerevisiae
histone lysine methyltransferase
-
 Saccharomyces cerevisiae
Rad9
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction failure to recruit Rad9 or Dot1 to histone H3 leads to an increase in Mec1 activation Saccharomyces cerevisiae
physiological function Dot1 and Rad9 inhibit single-stranded DNA accumulation at DSBs and uncapped telomeres, Dot1 contributes to checkpoint activation in response to low levels of telomere uncapping but is not essential with high levels of uncapping, Rad9 contributes to DNA damage metabolism because Rad9 inhibits the accumulation of single stranded DNA at uncapped telomeres Saccharomyces cerevisiae