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Intestinal MUC2 mucin supramolecular topology by packing and release resting on D3 domain assembly.

Artikel i vetenskaplig tidskrift
Författare Harriet E. Nilsson
Daniel Ambort
Malin Bäckström
Elisabeth Thomsson
Philip J B Koeck
Gunnar C. Hansson
Hans Hebert
Publicerad i Journal of molecular biology
Volym 426
Nummer/häfte 14
Sidor 2567-79
ISSN 1089-8638
Publiceringsår 2014
Publicerad vid Core Facilities, Mammalian Protein Expression
Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 2567-79
Språk en
Länkar dx.doi.org/10.1016/j.jmb.2014.04.02...
Ämnesord Animals, CHO Cells, Colon, chemistry, metabolism, Cricetulus, Green Fluorescent Proteins, genetics, metabolism, Humans, Imaging, Three-Dimensional, Intestines, metabolism, Microscopy, Electron, Mucin-2, chemistry, genetics, metabolism, Protein Conformation, Protein Structure, Tertiary, Recombinant Proteins, genetics, metabolism
Ämneskategorier Medicinska grundvetenskaper, Cell- och molekylärbiologi

Sammanfattning

MUC2 is the major gel-forming mucin of the colon forming a protective gel barrier organized into an inner stratified and an outer loose layer. The MUC2 N-terminus (D1-D2-D'D3 domains) has a dual function in building a net-like structure by disulfide-bonded trimerization and packing the MUC2 polymer into an N-terminal concatenated polygonal platform with the C-termini extending perpendicularly by pH- and calcium-dependent interactions. We studied the N-terminal D'D3 domain by producing three recombinant variants, with or without Myc tag and GFP (green fluorescent protein), and analyzed these by gel filtration, electron microscopy and single particle image processing. The three variants were all trimers when analyzed upon denaturing conditions but eluted as hexamers upon gel filtration under native conditions. Studies by electron microscopy and three-dimensional maps revealed cage-like structures with 2- and 3-fold symmetries. The structure of the MUC2 D3 domain confirms that the MUC2 mucin forms branched net-like structures. This suggests that the MUC2 mucin is stored with two N-terminal concatenated ring platforms turned by 180° against each other, implicating that every second unfolded MUC2 net in mature mucus is turned upside down.

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