Journal of Microbiology

Research Support, Non-U.S. Gov't

NOTE] Functional Analysis of a Hansenula polymorpha MNN2-2 Homologue Encoding a Putative UDP-N-acetylglucosamine Transporter Localized in the Endoplasmic Reticulum: Jeong-Nam Park , Jinho Choo , Hyun Ah Kang; J. Microbiol. 2011;49(6):1012-1017. Published online December 28, 2011; DOI: https://doi.org/10.1007/s12275-011-1520-4

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.

Search