Proteins of rough microsomal membranes related to ribosome binding. I. Identification of ribophorins I and II, membrane proteins characteristics of rough microsomes

@article{Kreibich1978ProteinsOR,
  title={Proteins of rough microsomal membranes related to ribosome binding. I. Identification of ribophorins I and II, membrane proteins characteristics of rough microsomes},
  author={G. Kreibich and B. Ulrich and D. Sabatini},
  journal={The Journal of Cell Biology},
  year={1978},
  volume={77},
  pages={464 - 487}
}
Rat liver rough microsomes (RM) contain two integral membrane proteins which are not found in smooth microsomes (SM) and appear to be related to the presence of ribosome-binding sites. These proteins, of molecular weight 65,000 and 63,000, were designated ribophorins I and II, respectively. They were not released from the microsomal membranes by alkali or acid treatment, or when the ribosomes were detached by incubation with puromycin in a high salt medium. The anionic detergent sodium… Expand
Proteins of rough microsomal membranes related to ribosome binding. II. Cross-linking of bound ribosomes to specific membrane proteins exposed at the binding sites
TLDR
Experiments with RM which contained only inactive ribosome showed that the presence of nascent chains was not necessary for the reversible cross-linking of ribosomes to the membranes, and suggest that ribophorins are in close proximity to the bound ribosomal- binding sites, as may be expected from components of the ribo-binding sites. Expand
Recovery of ribophorins and ribosomes in "inverted rough" vesicles derived from rat liver rough microsomes
TLDR
SDS PAGE analysis of the two vesicle subfractions demonstrated that, of all the integral microsomal membrane proteins, only ribophorins I and II were found exclusively in the inverted rough vesicles bearing ribosomes, consistent with the proposal that ribopharins are associated with the ribosomal binding sites characteristic of rough microsome membranes. Expand
Identification of ribophorins in rough microsomal membranes from different organs of several species.
Microsomes prepared from several animal sources were analyzed for the presence of proteins corresponding to the ribophorins (I and II) which have been previously characterized in rat liver roughExpand
Ribophorins I and II: membrane proteins characteristic of the rough endoplasmic reticulum.
TLDR
The presence of ribophorins as a characteristic feature of rough endoplamic reticulum (RER) membranes suggests that these proteins play an important functional role in the process by which nascent polypeptides are inserted into ER membranes. Expand
Spatial orientation of glycoproteins in membranes of rat liver rough microsomes. II. Transmembrane disposition and characterization of glycoproteins
TLDR
Rat liver microsomal glycoproteins were purified by affinity chromatography on concanavalin A Sepharose columns from membrane and content fractions, separated from rough microsomes (RM) treated with low concentrations of deoxycholate, and ribophorins I and II, two integral membrane proteins characteristic of RM, were found to be transmembrane gly coproteins. Expand
A membrane preparation that contains proteins characteristic of the rough endoplasmic reticulum
TLDR
A procedure for disassembling rat liver rough microsomes, which allows the purification of the rough endoplasmic reticulum (ER) membrane, which contains the docking protein and protein disulfide isomerase, and has conserved the functional capacity to remove co‐ and post‐translationally the signal peptide of pre‐secretory proteins. Expand
Segregation to Regions of the Endoplasmic Reticulum Ribophorins and Ribosomes. II. Rat Liver Subfractions Ribososmes of the Polypeptide Translocation Apparatus Containing Microsomal Contain Equimolar Amounts of Ribophorins and EUGENE E. MARCANTONIO,* ALAIN AMAR-COSTESEC,* and GERT KREIBICH*
Ribophorins I and II, two transmembrane glycoproteins characteristic of the rough endoplasmic reticulum (ER) are thought to be part of the translocation apparatus for proteins made on membrane boundExpand
Translocation and proteolytic processing of nascent secretory polypeptide chains: two functions associated with the ribosomal domain of the endoplasmic reticulum
TLDR
Several components of the endosplamic reticulum now appear to be segregated within restricted areas on either side of the membrane, and to make up a biochemically distinct domain, which is proposed to call the ribosomal domain in consideration of its contribution to protein biosynthesis by bound ribosomes. Expand
Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein
TLDR
The data here demonstrate conclusively that the initial events that lead to translocation and provide for its specificity are protein-protein (signal sequence plus ribosome with SRP) and not protein-lipid (Signal sequence with lipid bilayer) interactions. Expand
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Proteins of rough microsomal membranes related to ribosome binding. II. Cross-linking of bound ribosomes to specific membrane proteins exposed at the binding sites
TLDR
Experiments with RM which contained only inactive ribosome showed that the presence of nascent chains was not necessary for the reversible cross-linking of ribosomes to the membranes, and suggest that ribophorins are in close proximity to the bound ribosomal- binding sites, as may be expected from components of the ribo-binding sites. Expand
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TLDR
It appears that ribosomes are bound to membranes via two types of interactions: a direct one between the membrane and the large ribosomal subunit (labile at high KCl concentration) and an indirect one in which the nascent chain anchors the ribosome to the membrane (puromycin labile). Expand
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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