title: Effect of GTP-binding protein (YPT1 protein) on the enhanced yeast vacuolar activity.
abstract: Yeast GTP-binding protein (YPT1 protein) has been reported to function in the early stages of the secretory pathway. Particularly, YPT1 protein is observed to regulate both the endoplasmic reticulum-to-Golgi transport and the autophagy. Therefore, the YPT1 protein overexpressed in yeast vacuoles is expected to enhance antimicrobial and anticancer activity. The enhancement of yeast vacuolar activity under the overexpression of YPT1 was evaluated by the analysis of lysozyme activity, antimicrobial activity against Escherichia coli and Staphylococcus aureus, and MTT assay against HeLa cell lines. Additionally, the rise in concentration of some important proteinases inside the vacuole, such as proteinase A, proteinase B, and vacuolar carboxypeptidase Y (CPY) were also recorded using a 2DE technique. All results imply YPT1 involvement in the recruitment of some specific proteinases into vacuoles, which leads to the enhancement of vacuolar activity. Since these there proteinases belong to the CPY pathway, YPT1 is even believed to up-regulate this trafficking pathway in yeast cells. Future studies, however, should be carried out to discover the mechanisms that allow YPT1 to recruit these proteins into yeast vacuoles.
authors.affiliation: Department of Bioprocess Engineering, Chonbuk National University, 664-14 Duckjin-dong, Jeonju, 561-756, South Korea.
authors.forename: Le Minh
authors.initials: le M
authors.lastname: Tran
authors.affiliation: Department of Bioprocess Engineering, Chonbuk National University, 664-14 Duckjin-dong, Jeonju, 561-756, South Korea.
authors.forename: Seung Hyuck
authors.initials: SH
authors.lastname: Bang
authors.affiliation: Department of Chemical Engineering, Chonbuk National University, 664-14 Deokjin-dong, 1 Ga Deokjin-Gu, Jeonju, 561-756, South Korea.
authors.forename: Jihee
authors.initials: J
authors.lastname: Yoon
authors.affiliation: Department of Microbiology, Chungbuk National University, 410 Sungbong-Ro, Heungduk-Gu, Cheongju, 361-763, South Korea. kyh@chungbuk.ac.kr.
authors.forename: Yang-Hoon
authors.initials: YH
authors.lastname: Kim
authors.affiliation: Department of Bioprocess Engineering, Chonbuk National University, 664-14 Duckjin-dong, Jeonju, 561-756, South Korea. jihomin@jbnu.ac.kr.|Department of Chemical Engineering, Chonbuk National University, 664-14 Deokjin-dong, 1 Ga Deokjin-Gu, Jeonju, 561-756, South Korea. jihomin@jbnu.ac.kr.
authors.forename: Jiho
authors.initials: J
authors.lastname: Min
mesh_terms: D000890:Anti-Infective Agents / Q000494:pharmacology; D000970:Antineoplastic Agents / Q000494:pharmacology; D005656:Fungal Proteins / Q000494:pharmacology; D006367:HeLa Cells; D006801:Humans; D008855:Microscopy, Electron, Scanning; D009113:Muramidase / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism; D011995:Recombination, Genetic; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D014617:Vacuoles / Q000201:enzymology / Q000378:metabolism*; D020691:rab GTP-Binding Proteins / Q000378:metabolism*
chemical_list: D000890:Anti-Infective Agents; D000970:Antineoplastic Agents; D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D009113:Muramidase; D010447:Peptide Hydrolases; C060755:YPT1 protein, S cerevisiae; D020691:rab GTP-Binding Proteins
keywords: CPY pathway; GTP-binding protein; Lysosome; Trafficking pathway; Vacuole; YPT1