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Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in Saccharomyces cerevisiae

Piłsyk, Sebastian and Perlinska-Lenart, Urszula and Janik, Anna and Gryz, Elzbieta and Ajchler-Adamska, Marta and Kruszewska, Joanna S. (2020) Yil102c-A is a Functional Homologue of the DPMII Subunit of Dolichyl Phosphate Mannose Synthase in Saccharomyces cerevisiae. International Journal of Molecular Sciences, 21 (8938). ISSN 1422-0067

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Official URL: https://www.mdpi.com/1422-0067/21/23/8938

Abstract

: In a wide range of organisms, dolichyl phosphate mannose (DPM) synthase is a complex of tree proteins Dpm1, Dpm2, and Dpm3. However, in the yeast Saccharomyces cerevisiae, it is believed to be a single Dpm1 protein. The function of Dpm3 is performed in S. cerevisiae by the C-terminal transmembrane domain of the catalytic subunit Dpm1. Until present, the regulatory Dpm2 protein has not been found in S. cerevisiae. In this study, we show that, in fact, the Yil102c-A protein interacts directly with Dpm1 in S. cerevisiae and influences its DPM synthase activity. Deletion of the YIL102c-A gene is lethal, and this phenotype is reversed by the dpm2 gene from Trichoderma reesei. Functional analysis of Yil102c-A revealed that it also interacts with glucosylphosphatidylinositol-N-acetylglucosaminyl transferase (GPI-GnT), similar to DPM2 in human cells. Taken together, these results show that Yil102c-A is a functional homolog of DPMII from T. reesei and DPM2 from humans.

Item Type:Article
Subjects:Q Science > Q Science (General)
Q Science > QR Microbiology
Divisions:Laboratory of Fungal Glycobiology
ID Code:1937
Deposited By: prof dr hab Joanna S. Kruszewska
Deposited On:30 Nov 2020 11:19
Last Modified:30 Nov 2020 11:19

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