Proteasomal turnover of hepatitis C virus core protein is regulated by two distinct mechanisms: a ubiquitin-dependent mechanism and a ubiquitin-independent but PA28gamma-dependent mechanism.

We have previously reported on the ubiquitylation and degradation of hepatitis C virus core protein. Here we demonstrate that proteasomal degradation of the core protein is mediated by two distinct mechanisms. One leads to polyubiquitylation, in which lysine residues in the N-terminal region are preferential ubiquitylation sites.

[Two cases of severe necrotizing pneumonia caused by community-acquired methicillin-resistant Staphylococcus aureus].

We present 2 cases with severe necrotizing pneumonia due to community-acquired methicillin-resistant Staphylococcus aureus (CA-MRSA) infection. The patients were a 89-year-old man and a male student of 15 years of age. Chest X-rays and CT scans demonstrated multiple consolidations with cavitary lesions showing necrotizing pneumonia.

E6AP ubiquitin ligase mediates ubiquitylation and degradation of hepatitis C virus core protein.

Hepatitis C virus (HCV) core protein is a major component of viral nucleocapsid and a multifunctional protein involved in viral pathogenesis and hepatocarcinogenesis. We previously showed that the HCV core protein is degraded through the ubiquitin-proteasome pathway. However, the molecular machinery for core ubiquitylation is unknown.