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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Spremulli, Linda L. Kaushal, Prem S. Tung, Chang-shung Sharma, Manjuli R. Agrawal, Rajendra K. Booth, Timothy M. Haque, Emdadul M. Sanbonmatsu, Karissa Y. |
| Description | Author Affiliation: Kaushal PS ( Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY 12201); Sharma MR ( Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY 12201); Booth TM ( Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY 12201); Haque EM ( Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599); Tung CS ( Theoretical Biology and Biophysics, Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545); Sanbonmatsu KY ( Theoretical Biology and Biophysics, Theoretical Division, Los Alamos National Laboratory, Los Alamos, NM 87545); Spremulli LL ( Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599); Agrawal RK ( Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, NY 12201); |
| Abstract | The mammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing 13 membrane proteins that form essential components of the complexes involved in oxidative phosphorylation or ATP generation for the eukaryotic cell. The mammalian 55S mitoribosome contains significantly smaller rRNAs and a large mass of mitochondrial ribosomal proteins (MRPs), including large mito-specific amino acid extensions and insertions in MRPs that are homologous to bacterial ribosomal proteins and an additional 35 mito-specific MRPs. Here we present the cryo-EM structure analysis of the small (28S) subunit (SSU) of the 55S mitoribosome. We find that the mito-specific extensions in homologous MRPs generally are involved in inter-MRP contacts and in contacts with mito-specific MRPs, suggesting a stepwise evolution of the current architecture of the mitoribosome. Although most of the mito-specific MRPs and extensions of homologous MRPs are situated on the peripheral regions, they also contribute significantly to the formation of linings of the mRNA and tRNA paths, suggesting a tailor-made structural organization of the mito-SSU for the recruitment of mito-specific mRNAs, most of which do not possess a 5' leader sequence. In addition, docking of previously published coordinates of the large (39S) subunit (LSU) into the cryo-EM map of the 55S mitoribosome reveals that mito-specific MRPs of both the SSU and LSU are involved directly in the formation of six of the 15 intersubunit bridges. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 20 |
| Volume Number | 111 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2014-05-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Mitochondria Metabolism Ribosomes Ultrastructure Animals Binding Sites Cryoelectron Microscopy Cytoplasm GTP-Binding Proteins Image Processing, Computer-Assisted Liver Protein Conformation RNA, Messenger RNA, Ribosomal, 16S RNA, Transfer Ribosomal Proteins Research Support, N.I.H., Extramural Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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