Functional analysis of a <Emphasis Type="Italic">Hansenula polymorpha MNN2-2</Emphasis> homologue encoding a putative UDP-<Emphasis Type="Italic">N</Emphasis>-acetylglucosamine transporter localized in the endoplasmic reticulum |
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Authors: | Jeong-Nam Park Jinho Choo Hyun Ah Kang |
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Institution: | Department of Life Science, Research Center for Biomolecules and Biosystems, Chung-Ang University, Seoul 156-756, Republic of Korea. |
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Abstract: | The Kluyveromyces lactis UDP-GlcNAc transporter (KlMnn2-2p) is responsible for the biosynthesis of N-glycans containing N-acetylglucosamine. A putative gene of Hansenula polymorpha encoding a KlMnn2-2p homologue, HpMNN2-2, was identified and investigated for its function. The deletion mutant strain of HpMNN2-2 (Hpmnn2-2Δ) showed increased sensitivity to geneticin, hygromycin B, and tunicamycin. However, the Hpmnn2-2Δ strain exhibited increased resistance to Calcofluor white, an inhibitor of chitin biosynthesis, along with a reduced chitin
content. The localization of HpMnn2-2p at the endoplasmic reticulum-enriched membrane, different from the Golgi localization
of a K. lactis homologue, further supports the involvement of HpMnn2-2p in cell wall chitin biosynthesis. |
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