Journal
PLANT JOURNAL
Volume 80, Issue 5, Pages 809-822Publisher
WILEY
DOI: 10.1111/tpj.12671
Keywords
Arabidopsis thaliana; glycosyltransferase; Golgi apparatus; N-glycan processing; Nicotiana benthamiana; protein-protein interaction; transmembrane domain; type-II membrane protein
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Funding
- Austrian Science Fund [P23906-B20]
- Science and Technology Facilities Council Program
- Austrian Research Promotion Agency Laura Bassi Centres of Expertise Grant [822757]
- Austrian Science Fund (FWF) [P 23906] Funding Source: researchfish
- Austrian Science Fund (FWF) [P23906] Funding Source: Austrian Science Fund (FWF)
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Golgi-resident type-II membrane proteins are asymmetrically distributed across the Golgi stack. The intrinsic features of the protein that determine its subcompartment-specific concentration are still largely unknown. Here, we used a series of chimeric proteins to investigate the contribution of the cytoplasmic, transmembrane and stem region of Nicotiana benthamiana N-acetylglucosaminyltransferase I (GnTI) for its cis/medial-Golgi localization and for protein-protein interaction in the Golgi. The individual GnTI protein domains were replaced with those from the well-known trans-Golgi enzyme 2,6-sialyltransferase (ST) and transiently expressed in Nicotiana benthamiana. Using co-localization analysis and N-glycan profiling, we show that the transmembrane domain of GnTI is the major determinant for its cis/medial-Golgi localization. By contrast, the stem region of GnTI contributes predominately to homomeric and heteromeric protein complex formation. Importantly, in transgenic Arabidopsis thaliana, a chimeric GnTI variant with altered sub-Golgi localization was not able to complement the GnTI-dependent glycosylation defect. Our results suggest that sequence-specific features in the transmembrane domain of GnTI account for its steady-state distribution in the cis/medial-Golgi in plants, which is a prerequisite for efficient N-glycan processing in vivo.
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