Functional analysis of a Hansenula polymorpha MNN2-2 homologue encoding a putative UDP-N-acetylglucosamine transporter localized in the endoplasmic reticulumopen access
- Authors
- Park, Jeong-Nam; Choo, Jinho; Kang, Hyun Ah
- Issue Date
- Dec-2011
- Publisher
- MICROBIOLOGICAL SOCIETY KOREA
- Keywords
- Hansenula polymorpha; UDP-GlcNAc transporter; endoplasmic reticulum; chitin
- Citation
- JOURNAL OF MICROBIOLOGY, v.49, no.6, pp 1012 - 1017
- Pages
- 6
- Journal Title
- JOURNAL OF MICROBIOLOGY
- Volume
- 49
- Number
- 6
- Start Page
- 1012
- End Page
- 1017
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/21077
- DOI
- 10.1007/s12275-011-1520-4
- ISSN
- 1225-8873
1976-3794
- 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 (Hpmnn2-2 Delta) showed increased sensitivity to geneticin, hygromycin B, and tunicamycin. However, the Hpmnn2-2 Delta 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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