PubMed:24443562 JSONTXT 24 Projects

Annnotations TAB TSV DIC JSON TextAE

Id Subject Object Predicate Lexical cue
T1 0-118 DRI_Approach denotes The Saccharomyces cerevisiae Mlh1-Mlh3 heterodimer is an endonuclease that preferentially binds to Holliday junctions.
T2 119-240 DRI_Challenge denotes MutLγ, a heterodimer of the MutL homologues Mlh1 and Mlh3, plays a critical role during meiotic homologous recombination.
T3 241-503 DRI_Challenge denotes The meiotic function of Mlh3 is fully dependent on the integrity of a putative nuclease motif DQHAX2EX4E, inferring that the anticipated nuclease activity of Mlh1-Mlh3 is involved in the processing of joint molecules to generate crossover recombination products.
T4 504-713 DRI_Background denotes Although a vast body of genetic and cell biological data regarding Mlh1-Mlh3 is available, mechanistic insights into its function have been lacking due to the unavailability of the recombinant protein complex.
T5 714-802 DRI_Approach denotes Here we expressed the yeast Mlh1-Mlh3 heterodimer and purified it into near homogeneity.
T6 803-879 DRI_Approach denotes We show that recombinant MutLγ is a nuclease that nicks double-stranded DNA.
T7 880-990 DRI_Approach denotes We demonstrate that MutLγ binds DNA with a high affinity and shows a marked preference for Holliday junctions.
T8 991-1148 DRI_Outcome denotes We also expressed the human MLH1-MLH3 complex and show that preferential binding to Holliday junctions is a conserved capacity of eukaryotic MutLγ complexes.
T9 1149-1239 DRI_Outcome denotes Specific DNA recognition has never been observed with any other eukaryotic MutL homologue.
T10 1240-1332 DRI_Approach denotes MutLγ thus represents a new paradigm for the function of the eukaryotic MutL protein family.
T11 1333-1482 DRI_Outcome denotes We provide insights into the mode of Holliday junction recognition and show that Mlh1-Mlh3 prefers to bind the open unstacked Holliday junction form.
T12 1483-1608 DRI_Approach denotes This further supports the model where MutLγ is part of a complex acting on joint molecules to generate crossovers in meiosis.