Recent studies demonstrated that orb‐weaving spiders may alter web architectures, the amount of silk in webs, or the protein composition of silks in response to variation in amount or type of prey. In this study, we conducted food manipulations to examine three mechanisms by which orb‐weaving spiders may adjust the performance of webs to variation in prey by altering the architectures of webs, making structural changes to the diameters of silk threads, and manipulating the material properties or amino acid composition of silk fibers. We fed Nephila pilipes two different types of prey, crickets or flies, and then compared orb structure and the chemical and physical properties of major ampullate (MA) silk between groups. Prey type did not affect orb structures in N. pilipes, except for mesh size. However, MA silk diameter and the stiffness of orbs constructed by spiders fed crickets were significantly greater than for the fly group. MA fibers forcibly silked from N. pilipes fed crickets was significantly thicker, but less stiff, than silk from spiders fed flies. Spiders in the cricket treatment also produced MA silk with slightly, but statistically significantly, more serine than silk from spiders in the fly treatment. Percentages of other major amino acids (proline, glycine, and glutamine) did not differ between treatments. This study demonstrated that orb‐weaving spiders can simultaneously alter some structural and material properties of MA silk, as well as the physical characteristics of webs, in response to different types of prey.
Summary
Posttranslational modifications of histones play fundamental roles in many biological functions. Specifically, histone H4-K20 methylation is critical in DNA synthesis and repair. However, little is known about how these functions are regulated by the upstream stimuli. Here, we identify a tyrosine phosphorylation site at Y72 of histone H4, which facilitates recruitment of histone methyltransferases (HMTases), SET8 and SUV4-20H, to enhance its K20 methylation, thereby promoting DNA synthesis and repair. Phosphorylation-defective histone H4 mutant is deficient in K20 methylation, leading to reduced DNA synthesis, delayed cell cycle progression, and decreased DNA repair ability. Disrupting the interaction between epidermal growth factor receptor (EGFR) and histone H4 by Y72 peptide significantly reduced tumor growth. Furthermore, EGFR expression clinically correlates with histone H4-Y72 phosphorylation, H4-K20 mono-methylation, and the Ki-67 proliferation marker. These findings uncover a mechanism by which EGFR transduces signal to chromatin to regulate DNA synthesis and repair.
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