Title NOTE] Functional Analysis of a Hansenula polymorpha MNN2-2 Homologue Encoding a Putative UDP-N-acetylglucosamine Transporter Localized in the Endoplasmic Reticulum
Author Jeong-Nam Park, Jinho Choo, and Hyun Ah Kang*
Address Department of Life Science, Research Center for Biomolecules and Biosystems, Chung-Ang University, Seoul 156-756, Republic of Korea
Bibliography Journal of Microbiology, 49(6),1012-1017, 2011,
DOI
Key Words Hansenula polymorpha, UDP-GlcNAc transporter, endoplasmic reticulum, chitin
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.