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Your search keyword '"Shahrizal, Mohammad"' showing total 3 results
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3 results on '"Shahrizal, Mohammad"'

1. DNA Methylation of Human Choline Kinase Alpha Gene

Author

Cun See Too Wei, Ling Few Ling, Mohammad Shahrizal Mohammad Umar, Hiang Yee Yoke, Siti Aisyah Faten Mohamed Sa'dom, and Nur Farah Hani Azemi

Subjects
Multidisciplinary, Chemistry, 05 social sciences, Choline kinase alpha, Promoter, Methylation, Molecular biology, CpG site, 0502 economics and business, DNA methylation, Gene expression, 050211 marketing, Epigenetics, Gene, 050203 business & management
Abstract

Increased level of choline kinase (CK) is a common feature in cancers and inhibition of this enzyme has been applied as anticancer strategy. DNA methylation of gene promoter especially at CpG island is associated with suppression of gene expression. Despite the importance of CK especially the alpha isoform in cancer pathogenesis, epigenetic regulation of ckα expression has not been investigated. Hence, this study aimed to determine the effect of DNA methylation on ckα promoter activity and gene expression by using hypomethylating (5-aza) and methylating (budesonide) agents. The level of DNA methylation in the second CpG island of ckα promoter was determined by PCR-based method. 5-aza and budesonide increased the methylation of the selected CpG island compared to untreated control. Treatment with the drugs produced opposite effect, with 5-aza induced ckα promoter activity and gene expression while budesonide suppressed the promoter activity and mRNA level of this gene. Deletion of a region containing the second CpG island on ckα promoter resulted in significantly lower promoter activity. In conclusion, this study showed that DNA methylation could be one of the mechanisms that regulate the expression of ckα gene.

Published
2020

3. Structural Basis for the Function of the β-Barrel Assembly-Enhancing Protease BepA.

Author

Shahrizal, Mohammad, Daimon, Yasushi, Tanaka, Yoshiki, Hayashi, Yugo, Nakayama, Shintaro, Iwaki, Shigehiro, Narita, Shin-ichiro, Kamikubo, Hironari, Akiyama, Yoshinori, and Tsukazaki, Tomoya

Subjects
*PROTEOLYTIC enzymes, *PROTEINS, *BIOSYNTHESIS, *PROTEIN tags, *CRYSTAL structure
Abstract

Abstract The β-barrel assembly machinery (BAM) complex mediates the assembly of β-barrel membrane proteins in the outer membrane. BepA, formerly known as YfgC, interacts with the BAM complex and functions as a protease/chaperone for the enhancement of the assembly and/or degradation of β-barrel membrane proteins. To elucidate the molecular mechanism underlying the dual functions of BepA, its full-length three-dimensional structure is needed. Here, we report the crystal structure of full-length BepA at 2.6-Å resolution. BepA possesses an N-terminal protease domain and a C-terminal tetratricopeptide repeat domain, which interact with each other. Domain cross-linking by structure-guided introduction of disulfide bonds did not affect the activities of BepA in vivo , suggesting that the function of this protein does not involve domain rearrangement. The full-length BepA structure is compatible with the previously proposed docking model of BAM complex and tetratricopeptide repeat domain of BepA. Graphical Abstract Unlabelled Image Highlights • Crystal structure (2.6 Å) of full-length BepA, β-barrel assembly-enhancing protease BepA • Crystal structure represents both its functional and resting states. • Functional model of BepA was proposed. [ABSTRACT FROM AUTHOR]

Published
2019
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