Cellular localization

In silico characterization of 1,2-diacylglycerol cholinephosphotransferase and lysophospha­tidylcholine acyltransferase genes in Glycine max L. Merrill

C. S. Sousa, Barros, B. A., Barh, D., Ghosh, P., Azevedo, V., Barros, E. G., Moreira, M. A., Sousa, C. S., Barros, B. A., Barh, D., Ghosh, P., Azevedo, V., Barros, E. G., and Moreira, M. A., “In silico characterization of 1,2-diacylglycerol cholinephosphotransferase and lysophospha­tidylcholine acyltransferase genes in Glycine max L. Merrill”, vol. 15, p. -, 2016.

The enzymes 1,2-diacylglycerol cholinephosphotrans­ferase (CPT) and lysophosphatidylcholine acyltransferase (LPCAT) are important in lipid metabolism in soybean seeds. Thus, understand­ing the genes that encode these enzymes may enable their modification and aid the improvement of soybean oil quality. In soybean, the genes encoding these enzymes have not been completely described; there­fore, this study aimed to identify, characterize, and analyze the in silico expression of these genes in soybean.

Characteristics of Cyclin B and its potential role in regulating oogenesis in the red claw crayfish (Cherax quadricarinatus)

L. M. Wang, Lv, W. W., Zuo, D., Dong, Z. J., and Zhao, Y. L., “Characteristics of Cyclin B and its potential role in regulating oogenesis in the red claw crayfish (Cherax quadricarinatus)”, vol. 14, pp. 10786-10798, 2015.

Cyclin B is a regulatory subunit of maturation-promoting factor (MPF), which has a key role in the induction of meiotic maturation of oocytes. MPF has been studied in a wide variety of animal species; however, its expression in crustaceans is poorly characterized. In this study, the complete cDNA sequence of Cyclin B was cloned from the red claw crayfish, Cherax quadricarinatus, and its spatiotemporal expression profiles were analyzed. Cyclin B cDNA (1779 bp) encoded a 401 amino acid protein with a calculated molecular weight of 45.1 kDa.

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