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Sld5 has an independent role in maintaining the centrosome structure by resisting the microtubule-mediated forces during mitosis.
The authors show that GINS is a compact tetramer in solution as observed in crystal structures, but also forms a double-tetrameric population, detectable by electron microscopy.
Knockdown of SLD5 using small interfering RNA resulted in reduction of cell growth both in vitro and an in vivo xenograft model. Moreover, we found that high levels of SLD5 in bladder cancer cells result from downregulation of microRNA (miR)-370 that otherwise suppresses its expression.
Sld5 a component of GINS complex interacts with SIK1 and recruits it to the sites of DNA replication at the onset of S phase.
The C-terminal domains of the Sld5 and Psf1 subunits are connected by linker regions to the core complex, and the C-terminal domain of Sld5 is important for core complex assembly.
Attenuation of SLD5 expression results in marked DNA damage in both normal cells and cancer cells, suggesting that it protects against DNA damage.
Requirement of SLD5 for early embryogenesis.
These data suggest that PSF1 and SLD5 may cooperate in the proliferation of immature cell populations.
The yeast heterotetrameric GINS complex is made up of Sld5, Psf1 (GINS1\; MIM 610608), Psf2 (GINS2\; MIM 610609), and Psf3 (GINS3\; MIM 610610). The formation of the GINS complex is essential for the initiation of DNA replication in yeast and Xenopus egg extracts (Ueno et al., 2005
DNA replication complex GINS protein SLD5
, SLD5 homolog