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KMS1 and KMS2, two plant endoplasmic reticulum proteins involved in the early secretory pathway
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Wang, Pengwei, Hummel, Eric, Osterrieder, Anne, Meyer, Andreas J., Frigerio, Lorenzo, Sparkes, Imogen and Hawes, Chris. (2011) KMS1 and KMS2, two plant endoplasmic reticulum proteins involved in the early secretory pathway. Plant Journal, Vol.66 (No.4). pp. 613-628. ISSN 0960-7412
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Official URL: http://dx.doi.org/10.1111/j.1365-313X.2011.04522.x
Abstract
We have identified two endoplasmic reticulum (ER)-associated Arabidopsis proteins, KMS1 and KMS2, which are conserved among most species. Fluorescent protein fusions of KMS1 localised to the ER in plant cells, and over-expression induced the formation of a membrane structure, identified as ER whorls by electron microscopy. Hydrophobicity analysis suggested that KMS1 and KMS2 are integral membrane proteins bearing six transmembrane domains. Membrane protein topology was assessed by a redox-based topology assay (ReTA) with redox-sensitive GFP and confirmed by a protease protection assay. A major loop domain between transmembrane domains 2 and 3, plus the N- and C-termini were found on the cytosolic side of the ER. A C-terminal di(tri)-lysine motif is involved in retrieval of KMS1 and deletion led to a reduction of the GFP-KMS1 signal in the ER. Over-expression of KMS1/KMS2 truncations perturbed ER and Golgi morphology and similar effects were also seen when KMS1/KMS2 were knocked-down by RNA interference. Microscopy and biochemical experiments suggested that expression of KMS1/KMS2 truncations inhibited ER to Golgi protein transport.
| Item Type: | Journal Article |
|---|---|
| Divisions: | Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010) |
| Journal or Publication Title: | Plant Journal |
| Publisher: | Blackwell |
| ISSN: | 0960-7412 |
| Date: | May 2011 |
| Volume: | Vol.66 |
| Number: | No.4 |
| Page Range: | pp. 613-628 |
| Identification Number: | 10.1111/j.1365-313X.2011.04522.x |
| Status: | Peer Reviewed |
| Publication Status: | Published |
| Access rights to Published version: | Restricted or Subscription Access |
| Funder: | Biotechnology and Biological Sciences Research Council (BBSRC) , Oxford Brookes University |
| Grant number: | BB/D001080/1 (BBSRC) |
| URI: | http://wrap.warwick.ac.uk/id/eprint/42091 |
Data sourced from Thomson Reuters' Web of Knowledge
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