The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Export

@article{citeulike:4787852, abstract = {The early events in the life of newly synthesized proteins in the cellular environment are remarkably complex. Concurrently with their synthesis by the ribosome, nascent polypeptides are subjected to enzymatic processing, chaperone-assisted folding or targeting to translocation pores at membranes. The ribosome itself has a key role in these different tasks and governs the interplay between the various factors involved. Indeed, the ribosome serves as a platform for the spatially and temporally regulated association of enzymes, targeting factors and chaperones that act upon the nascent polypeptides emerging from the exit tunnel. Furthermore, the ribosome provides opportunities to coordinate the protein-synthesis activity of its peptidyl transferase center with the protein targeting and folding processes. Here we review the early co-translational events involving the ribosome that guide cytosolic proteins to their native state.}, author = {Kramer, G\"{u}nter and Boehringer, Daniel and Ban, Nenad and Bukau, Bernd}, citeulike-article-id = {4787852}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nsmb.1614}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/nsmb.1614}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/19491936}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=19491936}, doi = {10.1038/nsmb.1614}, issn = {1545-9985}, journal = {Nature structural \& molecular biology}, keywords = {co-translational, folding, protein, review, ribosome, role}, month = {June}, number = {6}, pages = {589--597}, posted-at = {2009-11-10 13:10:28}, priority = {2}, publisher = {Nature Publishing Group}, title = {The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins.}, url = {http://dx.doi.org/10.1038/nsmb.1614}, volume = {16}, year = {2009} }

TY - JOUR ID - citeulike:4787852 L3 - citeulike-article-id:4787852 N2 - The early events in the life of newly synthesized proteins in the cellular environment are remarkably complex. Concurrently with their synthesis by the ribosome, nascent polypeptides are subjected to enzymatic processing, chaperone-assisted folding or targeting to translocation pores at membranes. The ribosome itself has a key role in these different tasks and governs the interplay between the various factors involved. Indeed, the ribosome serves as a platform for the spatially and temporally regulated association of enzymes, targeting factors and chaperones that act upon the nascent polypeptides emerging from the exit tunnel. Furthermore, the ribosome provides opportunities to coordinate the protein-synthesis activity of its peptidyl transferase center with the protein targeting and folding processes. Here we review the early co-translational events involving the ribosome that guide cytosolic proteins to their native state. IS - 6 JF - Nature structural & molecular biology SN - 1545-9985 EP - 597 TI - The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. PB - Nature Publishing Group VL - 16 SP - 589 KW - co-translational KW - folding KW - protein KW - review KW - ribosome KW - role AU - Kramer, Günter AU - Boehringer, Daniel AU - Ban, Nenad AU - Bukau, Bernd PY - 2009/06// UR - http://dx.doi.org/10.1038/nsmb.1614 ER -