Structural insights to the RRM-domain of the glycine-rich RNA-binding protein from Sorghum bicolor and its role in cold stress tolerance in E. coli.

Sorghum bicolor Glycine-rich RNA-binding protein (SbGRBP), exhibit the ability to bind both single-stranded and double-stranded DNA. The expression of SbGRBP is regulated by heat stress, with the protein localizing to the nucleus and cytosol. The present study delves into the structure and ssDNA binding ability of its truncated version (SbGRBP1-119) which lacks glycine rich domain (GR).

Disorder in CENP-A tail-chaperone interaction facilitates binding with Ame1/Okp1 at the kinetochore.

The centromere is epigenetically marked by a histone H3 variant-CENP-A. The budding yeast CENP-A called Cse4, consists of an unusually long N-terminus that is known to be involved in kinetochore assembly. Its disordered chaperone, Scm3 is responsible for the centromeric deposition of Cse4 as well as in the maintenance of a segregation-competent kinetochore.

Catching Nucleosome by Its Decorated Tails Determines Its Functional States.

The fundamental packaging unit of chromatin, i.e., nucleosome, consists of ∼147 bp of DNA wrapped around a histone octamer composed of the core histones, H2A, H2B, H3, and H4, in two copies each.

Comparative analysis of SARS-CoV-2 envelope viroporin mutations from COVID-19 deceased and surviving patients revealed implications on its ion-channel activities and correlation with patient mortality.

One major obstacle in designing a successful therapeutic regimen to combat COVID-19 pandemic is the frequent occurrence of mutations in the SARS-CoV-2 resulting in patient to patient variations. Out of the four structural proteins of SARS-CoV-2 namely, spike, envelope, nucleocapsid and membrane, envelope protein governs the virus pathogenicity and induction of acute-respiratory-distress-syndrome which is the major cause of death in COVID-19 patients. These effects are facilitated by the viroporin (ion-channel) like activities of the envelope protein.