A dimeric structure for archaeal box C/D small ribonucleoproteins. Export

@article{citeulike:5773469, abstract = {Methylation of ribosomal RNA (rRNA) is required for optimal protein synthesis. Multiple 2'-O-ribose methylations are carried out by box C/D guide ribonucleoproteins [small ribonucleoproteins (sRNPs) and small nucleolar ribonucleoproteins (snoRNPs)], which are conserved from archaea to eukaryotes. Methylation is dictated by base pairing between the specific guide RNA component of the sRNP or snoRNP and the target rRNA. We determined the structure of a reconstituted and catalytically active box C/D sRNP from the archaeon Methanocaldococcus jannaschii by single-particle electron microscopy. We found that archaeal box C/D sRNPs unexpectedly formed a dimeric structure with an alternative organization of their RNA and protein components that challenges the conventional view of their architecture. Mutational analysis demonstrated that this di-sRNP structure was relevant for the enzymatic function of archaeal box C/D sRNPs.}, author = {Bleichert, Franziska and Gagnon, Keith T. and Brown, Bernard A. and Maxwell, E. Stuart and Leschziner, Andres E. and Unger, Vinzenz M. and Baserga, Susan J.}, citeulike-article-id = {5773469}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1176099}, citeulike-linkout-1 = {http://www.sciencemag.org/cgi/content/abstract/325/5946/1384}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/19745151}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=19745151}, day = {11}, doi = {10.1126/science.1176099}, issn = {1095-9203}, journal = {Science (New York, N.Y.)}, keywords = {image\_processing, sp, structure}, month = {September}, number = {5946}, pages = {1384--1387}, posted-at = {2009-09-23 10:26:22}, priority = {2}, title = {A dimeric structure for archaeal box C/D small ribonucleoproteins.}, url = {http://dx.doi.org/10.1126/science.1176099}, volume = {325}, year = {2009} }

TY - JOUR ID - citeulike:5773469 L3 - citeulike-article-id:5773469 N2 - Methylation of ribosomal RNA (rRNA) is required for optimal protein synthesis. Multiple 2'-O-ribose methylations are carried out by box C/D guide ribonucleoproteins [small ribonucleoproteins (sRNPs) and small nucleolar ribonucleoproteins (snoRNPs)], which are conserved from archaea to eukaryotes. Methylation is dictated by base pairing between the specific guide RNA component of the sRNP or snoRNP and the target rRNA. We determined the structure of a reconstituted and catalytically active box C/D sRNP from the archaeon Methanocaldococcus jannaschii by single-particle electron microscopy. We found that archaeal box C/D sRNPs unexpectedly formed a dimeric structure with an alternative organization of their RNA and protein components that challenges the conventional view of their architecture. Mutational analysis demonstrated that this di-sRNP structure was relevant for the enzymatic function of archaeal box C/D sRNPs. IS - 5946 JF - Science (New York, N.Y.) SN - 1095-9203 EP - 1387 TI - A dimeric structure for archaeal box C/D small ribonucleoproteins. VL - 325 SP - 1384 KW - image_processing KW - sp KW - structure AU - Bleichert, Franziska AU - Gagnon, Keith AU - Brown, Bernard AU - Maxwell, Stuart AU - Leschziner, Andres AU - Unger, Vinzenz AU - Baserga, Susan PY - 2009/09/11/ UR - http://dx.doi.org/10.1126/science.1176099 ER -