Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domain

Article Abstract:

The experiments that infer a radical reorientation of tyrosine-phosphorylated parallel STAT1 dimers to an antiparallel form, allowing easy access to a phosphatase, are reported. The analysis has suggested that spatial mobility of the N-terminal domain (ND) on its tether is needed for parallel-to-antiparallel reorientation of the phosphorylated core to allow efficient dephosphorylation and the ND has a vital role in promoting the dephosphorylation.

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YY1 DNA binding and PcG recruitment requires CtBP

Article Abstract:

Chromatin immunoprecipitation assays were performed in a transgenic Drosophila embryo system to determine whether YY1 could recruit Polycomb group (PcG) proteins to DNA. Results show that modulation of YY1 DNA binding by CtBP is a critical step in the recruitment of PcG proteins to DNA.

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Hop2/Mnd1 acts on two critical steps in Dmc1-promoted homologous pairing

Article Abstract:

The heterodimer complex formed by HOP2 and MND1 genes stimulates formation of synaptic complex by Dmc 1. The complex promotes DNA binding and stabilization of Dmc1-single stranded DNA presynaptic filaments.

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