Multiferroic heterostructures of Fe3O4/PZT (lead zirconium titanate), Fe3O4/PMN‐PT (lead magnesium niobate‐lead titanate) and Fe3O4/PZN‐PT (lead zinc niobate‐lead titanate) are prepared by spin‐spray depositing Fe3O4 ferrite film on ferroelectric PZT, PMN‐PT and PZN‐PT substrates at a low temperature of 90 °C. Strong magnetoelectric coupling (ME) and giant microwave tunability are demonstrated by a electrostatic field induced magnetic anisotropic field change in these heterostructures. A high electrostatically tunable ferromagnetic resonance (FMR) field shift up to 600 Oe, corresponding to a large microwave ME coefficient of 67 Oe cm kV−1, is observed in Fe3O4/PMN‐PT heterostructures. A record‐high electrostatically tunable FMR field range of 860 Oe with a linewidth of 330–380 Oe is demonstrated in Fe3O4/PZN‐PT heterostructure, corresponding to a ME coefficient of 108 Oe cm kV−1. Static ME interaction is also investigated and a maximum electric field induced squareness ratio change of 40% is observed in Fe3O4/PZN‐PT. In addition, a new concept that the external magnetic orientation and the electric field cooperate to determine microwave magnetic tunability is brought forth to significantly enhance the microwave tunable range up to 1000 Oe. These low temperature synthesized multiferroic heterostructures exhibiting giant electrostatically induced tunable magnetic resonance field at microwave frequencies provide great opportunities for electrostatically tunable microwave multiferroic devices.

Prim-pol is a recently identified DNA primase-polymerase belonging to the archaeao-eukaryotic primase (AEP) superfamily. Here, we characterize a previously unrecognized prim-pol in human cells, which we designate hPrimpol1 (human primasepolymerase 1). hPrimpol1 possesses primase and DNA polymerase activities in vitro, interacts directly with RPA1 and is recruited to sites of DNA damage and stalled replication forks in an RPA1-dependent manner. Cells depleted of hPrimpol1 display increased spontaneous DNA damage and defects in the restart of stalled replication forks. Both RPA1 binding and the primase activity of hPrimpol1 are required for its cellular function during DNA replication. Our results indicate that hPrimpol1 is a novel factor involved in the response to DNA replication stress.

The authors declare no competing financial interests. Data availability HTGTS V(D)J-seq, Hi-C, 3C-HTGTS, GRO-Seq and ChIP-Seq sequencing data reported in this study has been deposited in the GEO database under the accession number GSE130224. Specifically, HTGTS V(D)J-seq data is deposited in the GEO database under the accession number GSE130216 and is related to Fig. 1e-h; 2b, c; 3a-c, e; 4c; Extended Data Fig. 2c-e, g, h; 3e, f; 4a, c, d; 5a-c; 6c; 7d, e; 9b; and Supplementary Information Table 1&2. Hi-C data is deposited in the GEO database under accession number GSE134543 and is related to Extended Data Fig. 8a. 3C-HTGTS data is deposited in the GEO database under the accession number GSE130214 and is related to Fig. 3f; 4d; and Extended Data Fig. 8a; 9c; 10q, r. GRO-Seq data is deposited in the GEO database under the accession number GSE130215 and is related to Fig. 3d; 4b; and Extended Data Fig. 4e; 6d; 7f; 9b. ChIP-Seq data is deposited in the GEO database under the accession number GSE130213 and is related to Extended Data Fig. 8c, d; 9d. Code availability. HTGTS V(D)J-seq and 3C-HTGTS data was processed through published pipeline available at (http://robinmeyers.github.io/ transloc_pipeline/). Code for Hi-C data process is available at (github.com/aidenlab). GRO-Seq and ChIP-Seq were aligned to mm9 genome with bowtie2 v2.2.8 (http://bowtie-bio.sourceforge.net/bowtie2/index.shtml), processed by samtools v1.8 (https:// sourceforge.net/projects/samtools/files/samtools/1.8/) and generated graph files via RSeQC tool v2.6 (http://rseqc.sourceforge.net/ #bam2wig-py).