Search bioRxiv⌕ Search

Biology subjects

Aran-Guiu, X.

Publications and source records attributed to Aran-Guiu, X..

2 recordsLinked to original sources

HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation

Activation of client protein kinases by the HSP90 molecular chaperone system is affected by phosphorylation at multiple sites on HSP90, on the kinase specific co-chaperone CDC37, and the kinase client itself. Removal of regulatory phosphorylation from client kinases and their release from the HSP90-CDC37 system depends on a Ser/Thr phosphatase PP5, which associates with HSP90 via its N-terminal TPR domain. Here we present the cryoEM structure of the oncogenic protein kinase client BRAFV600E bound to HSP90-CDC37, showing how the V600E mutation favours BRAF association with HSP90-CDC37. Structures of HSP90-CDC37-BRAFV600E complexes with PP5, in autoinhibited and activated conformations, together with proteomic analysis of its phosphatase activity, reveal how PP5 is activated by recruitment to HSP90 complexes to comprehensively dephosphorylate client proteins.

biochemistry↗

Regulation of the MLH1-MLH3 endonuclease in meiosis

During prophase of the first meiotic division, cells deliberately break their DNA. These DNA breaks are repaired by homologous recombination, which facilitates proper chromosome segregation and enables reciprocal exchange of DNA segments between homologous chromosomes, thus promoting genetic diversity in the progeny1. A successful completion of meiotic recombination requires nucleolytic processing of recombination intermediates. Genetic and cellular data implicated a pathway dependent on the putative MLH1-MLH3 (MutL{gamma}) nuclease in generating crossovers, but mechanisms that lead to its activation were unclear2-4. Here, we have biochemically reconstituted key elements of this pro-crossover pathway. First, we show that human MSH4-MSH5 (MutS{gamma}), which was known to support crossing over5-7, binds branched recombination intermediates and physically associates with MutL{gamma}. This helps stabilize the ensemble at joint molecule structures and adjacent dsDNA. Second, we show that MutS{gamma} directly stimulates DNA cleavage by the MutL{gamma} endonuclease, which demonstrates a novel and unexpected function for MutS{gamma} in triggering crossing-over. Third, we find that MutL{gamma} activity is further stimulated by EXO1, but only when MutS{gamma} is present. Fourth, we also identify the replication factor C (RFC) and the proliferating cell nuclear antigen (PCNA) as additional components of the nuclease ensemble, and show that S. cerevisiae strains expressing PIP box-mutated MutL{gamma} present striking defects in forming crossovers. Finally, we show that the MutL{gamma}-MutS{gamma}-EXO1-RFC-PCNA nuclease ensemble preferentially cleaves DNA with Holliday junctions, but shows no canonical resolvase activity. Instead, the multilayered nuclease ensemble likely processes meiotic recombination intermediates by nicking dsDNA adjacent to junction points8. Since DNA nicking by MutL{gamma} is dependent on its co-factors, the asymmetric distribution of MutS{gamma} and RFC/PCNA on meiotic recombination intermediates may drive biased DNA cleavage. This unique mode of MutL{gamma} nuclease activation might explain crossover-specific processing of Holliday junctions within the meiotic chromosomal context3, 9.

biochemistry↗