Contributing factors to the oxidation-induced mutational landscape in human cells.

8-oxoguanine (8-oxoG) is a common oxidative DNA lesion that causes G > T substitutions. Determinants of local and regional differences in 8-oxoG-induced mutability across genomes are currently unknown. Here, we show DNA oxidation induces G > T substitutions and insertion/deletion (INDEL) mutations in human cells and cancers.

Case report of central serous chorioretinopathy with intraretinal fluid and normal fundus fluorescein and indocyanine green angiography.

A 73-year-old man was diagnosed with central serous chorioretinopathy (CSCR). He had atypical features including a normal indocyanine green angiography (ICG) and fundus fluorescein angiography (FFA), uncommon age group for initial diagnosis and a finding of intraretinal fluid. This case report is the first of our knowledge that exemplifies this type of unusual clinical presentation for CSCR.

STARD7 maintains intestinal epithelial mitochondria architecture, barrier integrity, and protection from colitis.

Susceptibility to inflammatory bowel diseases (IBDs), Crohn's disease (CD), and ulcerative colitis (UC) is linked with loss of intestinal epithelial barrier integrity and mitochondria dysfunction. Steroidogenic acute regulatory (StAR) protein-related lipid transfer (START) domain-containing protein 7 (STARD7) is a phosphatidylcholine-specific (PC-specific) lipid transfer protein that transports PC from the ER to the mitochondria, facilitating mitochondria membrane stabilization and respiration function. The aim of this study was to define the contribution of STARD7 in the regulation of the intestinal epithelial mitochondrial function and susceptibility to colitis.

Structural basis of gap-filling DNA synthesis in the nucleosome by DNA Polymerase β.

Single-strand breaks (SSBs) are one of the most prevalent forms of DNA damage found in the chromatinized genome and are repaired by direct single-strand break repair (SSBR) or base excision repair (BER). DNA polymerase beta (Pol β) is the primary enzyme responsible for processing the 1-nt gap intermediate in chromatin during SSBR and BER. However, the mechanism used by Pol β to process a 1-nt gap in the context of the nucleosome and chromatin remains poorly understood.

Structure of Blm10:13S proteasome intermediate reveals parallel assembly pathways for the proteasome core particle.

Proteasomes are formed by chaperone-assisted assembly of core particles (CPs) and regulatory particles (RPs). The CP chaperone dimer Pba1/Pba2 binds early to proteasome subunits, and is thought to be replaced by Blm10 to form Blm10:CP, which promotes ATP-independent degradation of disordered proteins. Here, we present evidence of distinct parallel assembly pathways for CP by solving five cryo-EM structures including a Blm10:13S pre-assembly intermediate.