KMS1 and KMS2, two plant endoplasmic reticulum proteins involved in the early secretory pathway
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 0960-7412Full text not available from this repository.
Official URL: http://dx.doi.org/10.1111/j.1365-313X.2011.04522.x
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|
|Page Range:||pp. 613-628|
|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)|
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