COVID-19 lockdown improved the health of coastal environment and enhanced the population of reef-fish.

Reduction in the impact of human-induced factors is capable of enhancing the environmental health. In view of COVID-19 pandemic, lockdowns were imposed in India. Travel, fishing, tourism and religious activities were halted, while domestic and industrial activities were restricted. Comparison of the pre- and post-lockdown data shows that water parameters such as turbidity, nutrient concentration and microbial levels have come down from pre- to post-lockdown period, and parameters such as dissolved oxygen levels, phytoplankton and fish densities have improved. The concentration of macroplastics has also dropped from the range of 138 ± 4.12 and 616 ± 12.48 items/100 m2 to 63 ± 3.92 and 347 ± 8.06 items/100 m2. Fish density in the reef areas has increased from 406 no. 250 m-2 to 510 no. 250 m-2. The study allows an insight into the benefits of effective enforcement of various eco-protection regulations and proper management of the marine ecosystems to revive their health for biodiversity conservation and sustainable utilization.

The nuclear receptor corepressor (N-CoR) contains three isoleucine motifs (I/LXXII) that serve as receptor interaction domains (IDs).

Unliganded thyroid hormone receptors (TRs) repress transcription through recruitment of corepressors, including nuclear receptor corepressor (N-CoR). We find that N-CoR contains three interaction domains (IDs) that bind to TR, rather than the previously reported two. The hitherto unrecognized ID (ID3) serves as a fully functional TR binding site, both in vivo and in vitro, and may be the most important for TR binding. Each ID motif contains a conserved hydrophobic core (I/LXXII) that resembles the hydrophobic core of nuclear receptor boxes (LXXLL), which mediates p160 coactivator binding to liganded nuclear receptors. Although the integrity of the I/LXXII motif is required for ID function, substitution of ID isoleucines with leucines did not allow ID peptides to bind to liganded TR, and substitution of NR box leucines with isoleucines did not allow NR box peptides to bind unliganded TR. This indicates that the binding preferences of N-CoR for unliganded TR and p160s for liganded TR are not dictated solely by the identity of conserved hydrophobic residues within their TR binding motifs. Examination of sequence conservation between IDs, and mutational analysis of individual IDs, suggests that they are comprised of the central hydrophobic core and distinct adjacent sequences that may make unique contacts with the TR surface. Accordingly, a hybrid peptide that contains distinct adjacent sequences from ID3 and ID1 shows enhanced binding to TR.