Digital deception: legal questions surround new “YouTube Kids” app

As the YouTube Kids app was launched in November 2015 in the UK and Ireland, nine months after it hit the US market, Dale Kunkel discusses how Google is stirring the debate on what is and what isn’t acceptable when it comes to advertising to children. In April 2015, Dale partnered with a coalition of 10 public interest and child advocacy groups to file a formal complaint with the Federal Trade Commission against YouTube Kids. Dale is Professor of Communication at the University of Arizona and he studies the effects of violence, sexual content, and advertising on young people

Sex on TV 2

Part of a series that examines the nature and extent of sexual messages conveyed on TV. Tracks changes that occur over time in the treatment of sexual topics, including references to possible risks or responsibilities. Based on a 1999-2000 program sample

Sex on TV 3

Part of a series that examines the nature and extent of sexual messages conveyed on TV. Tracks changes that occur over time in the treatment of sexual topics, including references to possible risks or responsibilities. Based on a 2001-2002 program sampl

Sex on TV: Content and Context

Part of a series that examines the nature and extent of sexual messages conveyed on American television. Focuses on references to contraception, safer sex, and waiting to have sex. Based on a sample of 1997-1998 programs

Sex on TV 4

Part of a series that examines the nature and extent of sexual messages conveyed on TV. Tracks changes that occur over time in the treatment of sexual topics, including references to possible risks or responsibilities. Based on a 2003-2004 program sample

Structural accommodation of ribonucleotide incorporation by the DNA repair enzyme polymerase Mu

While most DNA polymerases discriminate against ribonucleotide triphosphate (rNTP) incorporation very effectively, the Family X member DNA polymerase μ (Pol μ) incorporates rNTPs almost as efficiently as deoxyribonucleotides. To gain insight into how this occurs, here we have used X-ray crystallography to describe the structures of pre- and post-catalytic complexes of Pol μ with a ribonucleotide bound at the active site. These structures reveal that Pol μ binds and incorporates a rNTP with normal active site geometry and no distortion of the DNA substrate or nucleotide. Moreover, a comparison of rNTP incorporation kinetics by wildtype and mutant Pol μ indicates that rNTP accommodation involves synergistic interactions with multiple active site residues not found in polymerases with greater discrimination. Together, the results are consistent with the hypothesis that rNTP incorporation by Pol μ is advantageous in gap-filling synthesis during DNA double strand break repair by nonhomologous end joining, particularly in nonreplicating cells containing very low deoxyribonucleotide concentrations

Sustained active site rigidity during synthesis by human DNA polymerase μ

DNA polymerase mu (Pol μ) is the only template-dependent human DNA polymerase capable of repairing double strand DNA breaks (DSBs) with unpaired 3′-ends in non-homologous end joining (NHEJ). To probe this function, we structurally characterized Pol μ’s catalytic cycle for single nucleotide incorporation. These structures indicate that, unlike other template-dependent DNA polymerases, there are no large-scale conformational changes in protein subdomains, amino acid side chains, or DNA upon dNTP binding or catalysis. Instead, the only major conformational change is seen earlier in the catalytic cycle, when the flexible Loop1 region repositions upon DNA binding. Pol μ variants with changes in Loop1 have altered catalytic properties and are partially defective in NHEJ. The results indicate that specific Loop1 residues contribute to Pol μ’s unique ability to catalyze template-dependent NHEJ of DSBs with unpaired 3′-ends

Competition between neighbouring topogenic signals during membrane protein insertion into the ER membrane

To better define the mechanism of membrane protein insertion into the membrane of the endoplasmic reticulum, we measured the kinetics of translocation across microsomal membranes of the N-terminal lumenal tail and the lumenal domain following the second transmembrane segment (TM2) in the multispanning mouse protein Cig30. In the wild-type protein, the N-terminal tail translocates across the membrane before the downstream lumenal domain. Addition of positively charged residues to the N-terminal tail dramatically slows down its translocation and allows the downstream lumenal domain to translocate at the same time as or even before the N-tail. When TM2 is deleted, or when the loop between TM1 and TM2 is lengthened, addition of positively charged residues to the N-terminal tail causes TM1 to adopt an orientation with its N-terminal end in the cytoplasm. We suggest that the topology of the TM1-TM2 region of Cig30 depends on a competition between TM1 and TM2 such that the transmembrane segment that inserts first into the ER membrane determines the final topology

A Gradient of Template Dependence Defines Distinct Biological Roles for Family X Polymerases in Nonhomologous End Joining

Three Pol X family members have been linked to nonhomologous end joining (NHEJ) in mammals. Template-independent TdT promotes diversity during NHEJ-dependent repair of V(D)J recombination intermediates, but the roles of the template-dependent polymerases mu and lambda in NHEJ remain unclear. We show here that pol mu and pol lambda are similarly recruited by NHEJ factors to fill gaps when ends have partially complementary overhangs, suggesting equivalent roles promoting accuracy in NHEJ. However, only pol mu promotes accuracy during immunoglobulin kappa recombination. This distinctive in vivo role correlates with the TdT-like ability of pol mu, but not pol lambda, to act when primer termini lack complementary bases in the template strand. However, unlike TdT, synthesis by pol mu in this context is primarily instructed by a template from another DNA molecule. This apparent gradient of template dependence is largely attributable to a small structural element that is present but different in all three polymerases