Ribosomal protein S19-binding domain provides insights into hantavirus nucleocapsid protein-mediated translation initiation mechanism

Tula Hantavirus Nucleocapsid Protein

Hantavirus nucleocapsid protein oligomerization.

Hantaviruses are enveloped, negative-strand RNA viruses which can be lethal to humans, causing either a hemorrhagic fever with renal syndrome or a hantaviral pulmonary syndrome. The viral genomes consist of three RNA segments: the L segment encodes the viral polymerase, the M segment encodes the viral surface glycoproteins G1 and G2, and the S segment encodes the nucleocapsid (N) protein. The N...

Fasting Reduces the Binding between Sugar and Protein; New Insights into Diabetic Complications

Fasting has numerous biological, physical and mental health advantages or that as some physicians cure their patients by prescribing fasting to them. Fasting protects people from many diseases such as cancer, cardiovascular diseases, and diabetes complications. The main health-promoting effects of fasting are increased production of neurotrophic factors, neuroendocrine activation, hormetic stre...

Ribosomal protein S19 expression during erythroid differentiation.

The gene encoding ribosomal protein S19 (RPS19) has been shown to be mutated in 25% of the patients affected by Diamond-Blackfan anemia (DBA), a congenital erythroblastopenia. As the role of RPS19 in erythropoiesis is still to be defined, we performed studies on RPS19 expression during terminal erythroid differentiation. Comparative analysis of the genomic sequences of human and mouse RPS19 gen...

Translation initiation mediated by nuclear cap-binding protein complex

In mammals, cap-dependent translation of mRNAs is initiated by two distinct mechanisms: cap-binding complex (CBC; a heterodimer of CBP80 and 20)-dependent translation (CT) and eIF4E-dependent translation (ET). Both translation initiation mechanisms share common features in driving cap- dependent translation; nevertheless, they can be distinguished from each other based on their molecular featur...