Palmer amaranth is a difficult-to-control broadleaf weed that infests corn and soybean fields in south-central and southwestern Nebraska and several other states in the United States. The objectives of this research were to confirm triazine and 4-hydroxyphenylpyruvate dioxygenase (HPPD)-inhibiting herbicide-resistant Palmer amaranth in Nebraska and to determine sensitivity and efficacy of POST-applied corn herbicides for control of resistant and susceptible Palmer amaranth biotypes. Seeds from a putative HPPD-resistant Palmer amaranth biotype from Fillmore County, NE were collected from a seed corn production field in fall 2010. The response of Palmer amaranth biotypes to 12 rates (0 to 12×) of mesotrione, tembotrione, topramezone, and atrazine was evaluated in a dose–response bioassay in a greenhouse. On the basis of the values at the 90% effective dose (ED90) level, the analysis showed a 4- to 23-fold resistance depending upon the type of HPPD-inhibiting herbicide being investigated and susceptible biotype used for comparison. This biotype also had a 9- to 14-fold level of resistance to atrazine applied POST. Results of a POST-applied herbicide efficacy study suggested a synergistic interaction between atrazine and HPPD-inhibiting herbicides that resulted in > 90% control of all Palmer amaranth biotypes. The resistant biotype had a reduced sensitivity to acetolactate synthase inhibiting herbicides (halosulfuron and primisulfuron), a photosystem-II inhibitor (bromoxynil), and a protoporphyrinogen oxidase inhibitor (fluthiacet-methyl). Palmer amaranth biotypes were effectively controlled (≥ 90%) with glyphosate, glufosinate, and dicamba, whereas 2,4-D ester provided 81 to 83% control of the resistant biotype and > 90% control of both susceptible biotypes.

Liquid-liquid phase separation (LLPS) of proteins and nucleic acids has emerged as an important phenomenon in membraneless intracellular organization. We demonstrate that the linker histone H1 condenses into liquid-like droplets in the nuclei of HeLa cells. The droplets, observed during the interphase of the cell cycle, are colocalized with DNA-dense regions indicative of heterochromatin. In vitro, H1 readily undergoes LLPS with both DNA and nucleosomes of varying lengths but does not phase separate in the absence of DNA. The nucleosome core particle maintains its structural integrity inside the droplets, as demonstrated by FRET. Unexpectedly, H2A also forms droplets in the presence of DNA and nucleosomes in vitro, whereas the other core histones precipitate. The phase diagram of H1 with nucleosomes is invariant to the nucleosome length at physiological salt concentration, indicating that H1 is capable of partitioning large segments of DNA into liquid-like droplets. Of the proteins tested (H1, core histones, and the heterochromatin protein HP1a), this property is unique to H1. In addition, free nucleotides promote droplet formation of H1 nucleosome in a nucleotide-dependent manner, with droplet formation being most favorable with ATP. Although LLPS of HP1a is known to contribute to the organization of heterochromatin, our results indicate that H1 also plays a role. Based on our study, we propose that H1 and DNA act as scaffolds for phase-separated heterochromatin domains.

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