Life-Course Partnership Status and Biomarkers in Midlife: Evidence From the 1958 British Birth Cohort.

Objectives We examined the association between trajectories of partnership status over the life course and objectively measured health indicators in midlife. Methods We used data from 4 waves (1981, 1991, 2000, and 2002-2004) of the British National Child Development Study (NCDS), a prospective cohort study that includes all people born in Britain during 1 week in March 1958 (n = 18 558). Results After controlling for selection attributable to early-life and early-adulthood characteristics, we found that life-course trajectories of partnership status were associated with hemostatic and inflammatory markers, the prevalence of metabolic syndrome and respiratory function in midlife. Never marrying or cohabiting was negatively associated with health in midlife for both genders, but the effect was more pronounced in men. Women who had married in their late 20s or early 30s and remained married had the best health in midlife. Men and women in cohabiting unions had midlife health outcomes similar to those in formal marriages. Conclusions Partnership status over the life course has a cumulative effect on a wide range of objectively measured health indicators in midlife

Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad

Removal and repair of DNA damage by the nucleotide excision repair pathway requires two sequential incision reactions, which are achieved by the endonuclease UvrC in eubacteria. Here, we describe the crystal structure of the C-terminal half of UvrC, which contains the catalytic domain responsible for 5′ incision and a helix–hairpin–helix–domain that is implicated in DNA binding. Surprisingly, the 5′ catalytic domain shares structural homology with RNase H despite the lack of sequence homology and contains an uncommon DDH triad. The structure also reveals two highly conserved patches on the surface of the protein, which are not related to the active site. Mutations of residues in one of these patches led to the inability of the enzyme to bind DNA and severely compromised both incision reactions. Based on our results, we suggest a model of how UvrC forms a productive protein–DNA complex to excise the damage from DNA