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Proceedings of the Japan Academy, Ser. B, Physical and Biological Sciences


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The Proceedings of the Japan Academy, Series B was founded in 1912 as the Proceedings of the Imperial Academy by the then Imperial Academy of Japan (now the Japan Academy). The Journal was split to the Proceedings of the Japan Academy, Series A and Series B in 1977. PJA Series B publishes reviews and original articles in broad fields of natural sciences, such as chemistry, physics, astronomy, earth sciences, biology, engineering, agricultural sciences and medical sciences. All manuscripts are evaluated at least by two reviewers. Ten issues are published per year. The entire content is now freely available online through J-STAGE.

Vol. 92 No. 10 (2016)

Peroxisome biogenesis and human peroxisome-deficiency disorders
Proc. Jpn. Acad., Ser. B, Vol. 92, 463-477 (2016) [Abstract and Full Text]
Calcium inhibition as an intracellular signal for actin–myosin interaction
Kazuhiro KOHAMA
Proc. Jpn. Acad., Ser. B, Vol. 92, 478-498 (2016) [Abstract and Full Text]
Original Article
Both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in Physcomitrella patens
Yoshiko TAKAHASHI, Katsuaki TAKECHI, Susumu TAKIO, Hiroyoshi TAKANO
Proc. Jpn. Acad., Ser. B, Vol. 92, 499-508 (2016) [Abstract and Full Text]
Cover Illustration
Identification of genes that are essential for peroxisome assembly and responsible for peroxisome biogenesis disorders
  Peroxisomes have important roles in maintaining homeostasis in humans. This is highlighted by fatal genetic disorders in peroxisome biogenesis. This disorder includes Zellweger syndrome, which is associated with impaired brain development, hypomyelination in the central nerve system, and progressive loss of hearing and vision. To investigate biogenesis of peroxisomes and its disorders, Fujiki and his colleagues mutagenized Chinese hamster ovary (CHO-K1) cells, and isolated a dozen of mutant cell lines that were defective in various processes of the peroxisome assembly. They then applied the forward genetics or expression cloning strategy to isolate genes (PEXs) that were involved in the peroxisome assembly. This invaluably contributed to identify the genes responsible for human diseases caused by the impaired peroxisome biogenesis. In pages 463-477 of this issue, Fujiki reviews the field of peroxisome biogenesis.

  Front cover: Identification of the gene that is mutated in a patient of Zellweger syndrome.
  In upper 4 panels, the wild-type CHO-K1 and its mutant (Z65) that was defective in importing peroxisome matrix proteins were stained with an antibody to peroxisomal membrane protein PMP70 (a and b) or antibody against PTS1 peptide of peroxisomal matrix proteins (c and d). In Z65, PMP70 was localized in peroxisomes, but proteins carrying the PTS1 were not in the peroxisomes, indicating that Z65 is defective in transporting matrix proteins into peroxisome. In lower panels, the Z65 cell line (e) and a fibroblast cell line from a Zellweger patient (CG10 ZS) (f) were transformed with PEX2 gene, and stained with an antibody against catalase. Localization of catalases in peroxisomes of PEX2-transformed cells indicates that Z65 CHO cells and CG10 ZS human cells have a mutation in PEX2 gene, and PEX2 protein is essential for importing peroxisome matrix proteins such as catalase into peroxisomes. Scale bar, 20 µm.

Shigekazu Nagata
Member of the Japan Academy

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