scholarly journals A receptor component of the chloroplast protein translocation machinery

Science ◽  
1994 ◽  
Vol 266 (5193) ◽  
pp. 1989-1992 ◽  
Author(s):  
S Hirsch ◽  
E Muckel ◽  
F Heemeyer ◽  
G von Heijne ◽  
J Soll
Keyword(s):  
Protein Translocation ◽  
Chloroplast Protein ◽  
Receptor Component

scholarly journals Calcium regulation of chloroplast protein translocation is mediated by calmodulin binding to Tic32

2006 ◽  
Vol 103 (43) ◽  
pp. 16051-16056 ◽  
Author(s):  
F. Chigri ◽  
F. Hormann ◽  
A. Stamp ◽  
D. K. Stammers ◽  
B. Bolter ◽  
...  
Keyword(s):  
Protein Translocation ◽  
Calcium Regulation ◽  
Calmodulin Binding ◽  
Chloroplast Protein

Spatial localization of unknown proteins in the endoplasmic reticulum predicts functions

2007 ◽  
Vol 30 (4) ◽  
pp. 84
Author(s):  
Michael D. Jain ◽  
Hisao Nagaya ◽  
Annalyn Gilchrist ◽  
Miroslaw Cygler ◽  
John J.M. Bergeron
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Protein Synthesis ◽  
Protein Function ◽  
Protein Translocation ◽  
Spatial Localization ◽  
Predict Protein Function ◽  
Insight Into ◽  
Soluble Fractions ◽  
Er Membrane

Protein synthesis, folding and degradation functions are spatially segregated in the endoplasmic reticulum (ER) with respect to the membrane and the ribosome (rough and smooth ER). Interrogation of a proteomics resource characterizing rough and smooth ER membranes subfractionated into cytosolic, membrane, and soluble fractions gives a spatial map of known proteins involved in ER function. The spatial localization of 224 identified unknown proteins in the ER is predicted to give insight into their function. Here we provide evidence that the proteomics resource accurately predicts the function of new proteins involved in protein synthesis (nudilin), protein translocation across the ER membrane (nicalin), co-translational protein folding (stexin), and distal protein folding in the lumen of the ER (erlin-1, TMX2). Proteomics provides the spatial localization of proteins and can be used to accurately predict protein function.

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