Being "easy": Women's desire to accept help in later life.

This article examines the concept of being "easy" as a quality that female caregivers aspire to as they envision their potential care in later life. It draws on data from a qualitative study exploring the significance of caregiving to adult daughters' perspectives and plans for their own aging. Caregivers' experiences differ based upon their perception of how easy or difficult it was to care for their loved one. The former exemplifies a positive way to approach aging and the receiving of care. Being easy describes an attitude that these caregivers desired for their own later life.

"Keep dignity intact": exploring desires for quality long-term care among midlife women.

The purpose of this qualitative study was to provide in-depth descriptions of preferences for receipt of long-term care among a small sample of information-rich cases. The participants in this study, women in late midlife caring for a parent or parent-in-law, expressed where they would prefer to receive care, who they would want to provide care, and personal traits that would be important in a caregiver. A major theme centered personal characteristics these women would want in a caregiver, traits such as empathy, sensitivity, and knowledgeable about elder care. Implications for social work practice are discussed.

Binding of two DNA molecules by type II topoisomerases for decatenation.

Topoisomerases (topos) maintain DNA topology and influence DNA transaction processes by catalysing relaxation, supercoiling and decatenation reactions. In the cellular milieu, division of labour between different topos ensures topological homeostasis and control of central processes. In Escherichia coli, DNA gyrase is the principal enzyme that carries out negative supercoiling, while topo IV catalyses decatenation, relaxation and unknotting. DNA gyrase apparently has the daunting task of undertaking both the enzyme functions in mycobacteria, where topo IV is absent. We have shown previously that mycobacterial DNA gyrase is an efficient decatenase. Here, we demonstrate that the strong decatenation property of the enzyme is due to its ability to capture two DNA segments in trans. Topo IV, a strong dedicated decatenase of E. coli, also captures two distinct DNA molecules in a similar manner. In contrast, E. coli DNA gyrase, which is a poor decatenase, does not appear to be able to hold two different DNA molecules in a stable complex. The binding of a second DNA molecule to GyrB/ParE is inhibited by ATP and the non-hydrolysable analogue, AMPPNP, and by the substitution of a prominent positively charged residue in the GyrB N-terminal cavity, suggesting that this binding represents a potential T-segment positioned in the cavity. Thus, after the GyrA/ParC mediated initial DNA capture, GyrB/ParE would bind efficiently to a second DNA in trans to form a T-segment prior to nucleotide binding and closure of the gate during decatenation.