A novel fluorescence-activated cell sorting (FACS)-based screening identified ATG14, the gene required for pexophagy in the methylotrophic yeast.

Pexophagy is a type of autophagy that selectively degrades peroxisomes and can be classified as either macropexophagy or micropexophagy. During macropexophagy, individual peroxisomes are sequestered by pexophagosomes and transported to the vacuole for degradation, while in micropexophagy, peroxisomes are directly engulfed by the septated vacuole. To date, some autophagy-related genes (ATGs) required for pexophagy have been identified through plate-based assays performed primarily under micropexophagy-induced conditions.

Crosslinker-Based Regulation of Swelling Behavior of Poly(-isopropylacrylamide) Gels in a Post-Polymerization Crosslinking System.

A fundamental understanding of the effect of a crosslinker on gel properties is important for the design of novel soft materials because a crosslinking is a key component of polymer gels. We focused on post-polymerization crosslinking (PPC) system utilizing activated ester chemistry, which is a powerful tool due to structural diversity of diamine crosslinkers and less susceptibility to solvent effect compared to conventional divinyl crosslinking system, to systematically evaluate the crosslinker effect on the gel properties. A variety of alkyldiamine crosslinkers was employed for the synthesis of poly(-isopropylacrylamide) (PNIPAAm) gels and it was clarified that the length of alkyl chains of diamine crosslinkers strongly affected the gelation reaction and the swelling behavior.

Identification and characterization of a sulfoglycosidase from Bifidobacterium bifidum implicated in mucin glycan utilization.

Human gut symbiont bifidobacteria possess carbohydrate-degrading enzymes that act on the O-linked glycans of intestinal mucins to utilize those carbohydrates as carbon sources. However, our knowledge about mucin type O-glycan degradation by bifidobacteria remains fragmentary, especially regarding how they decompose sulfated glycans, which are abundantly found in mucin sugar-chains. Here, we examined the abilities of several Bifidobacterium strains to degrade a sulfated glycan substrate and identified a 6-sulfo-β-d-N-acetylglucosaminidase, also termed sulfoglycosidase, encoded by bbhII from Bifidobacterium bifidum JCM 7004.