» Articles » PMID: 25797916

The 55S Mammalian Mitochondrial Ribosome and Its TRNA-exit Region

Overview
Journal Biochimie
Specialty Biochemistry
Date 2015 Mar 24
PMID 25797916
Citations 8
Authors
Affiliations
Soon will be listed here.
Abstract

Mitochondria carry their own genetic material and gene-expression machinery, including ribosomes, which are responsible for synthesizing polypeptides that form essential components of the complexes involved in oxidative phosphorylation (or ATP generation) for the eukaryotic cell. Mitochondrial ribosomes (mitoribosomes) are quite divergent from cytoplasmic ribosomes in both composition and structure even as their main functional cores, such as the mRNA decoding and peptidyl transferase sites, are highly conserved. Remarkable progress has been made recently towards understanding the structure of mitoribosomes, by obtaining high-resolution cryo-electron microscopic (cryo-EM) maps. These studies confirm previous structural findings that had revealed that a significant reduction in size of ribosomal RNAs has caused topological changes in some of the functionally relevant regions, including the transfer RNA (tRNA)-binding sites and the nascent polypeptide-exit tunnel, within the structure of the mammalian mitoribosome. In addition, these studies provide unprecedented detailed views of the molecular architecture of those regions. In this review, we summarize the current state of knowledge of the structure of the mammalian mitoribosome and describe the molecular environment of its tRNA-exit region.

Citing Articles

Combined Transcriptome and Proteome Leukocyte's Profiling Reveals Up-Regulated Module of Genes/Proteins Related to Low Density Neutrophils and Impaired Transcription and Translation Processes in Clinical Sepsis.

Leite G, Ferreira B, Tashima A, Nishiduka E, Cunha-Neto E, Brunialti M Front Immunol. 2021; 12:744799.

PMID: 34594344 PMC: 8477441. DOI: 10.3389/fimmu.2021.744799.


Mitochondrial Protein Translation: Emerging Roles and Clinical Significance in Disease.

Wang F, Zhang D, Zhang D, Li P, Gao Y Front Cell Dev Biol. 2021; 9:675465.

PMID: 34277617 PMC: 8280776. DOI: 10.3389/fcell.2021.675465.


Expression profiling of mitochondria-associated microRNAs during osteogenic differentiation of human MSCs.

Zheng H, Liu J, Yu J, McAlinden A Bone. 2021; 151:116058.

PMID: 34144232 PMC: 8944210. DOI: 10.1016/j.bone.2021.116058.


Regulation of translation by one-carbon metabolism in bacteria and eukaryotic organelles.

Shetty S, Varshney U J Biol Chem. 2020; 296:100088.

PMID: 33199376 PMC: 7949028. DOI: 10.1074/jbc.REV120.011985.


Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation.

Koripella R, Sharma M, Bhargava K, Datta P, Kaushal P, Keshavan P Nat Commun. 2020; 11(1):3830.

PMID: 32737313 PMC: 7395135. DOI: 10.1038/s41467-020-17715-2.


References
1.
Amunts A, Brown A, Bai X, Llacer J, Hussain T, Emsley P . Structure of the yeast mitochondrial large ribosomal subunit. Science. 2014; 343(6178):1485-1489. PMC: 4046073. DOI: 10.1126/science.1249410. View

2.
Mears J, Sharma M, Gutell R, McCook A, Richardson P, Caulfield T . A structural model for the large subunit of the mammalian mitochondrial ribosome. J Mol Biol. 2006; 358(1):193-212. PMC: 3495566. DOI: 10.1016/j.jmb.2006.01.094. View

3.
Cavdar Koc E, Burkhart W, Blackburn K, Moseley A, Spremulli L . The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present. J Biol Chem. 2001; 276(22):19363-74. DOI: 10.1074/jbc.M100727200. View

4.
OBrien T . Evolution of a protein-rich mitochondrial ribosome: implications for human genetic disease. Gene. 2002; 286(1):73-9. DOI: 10.1016/s0378-1119(01)00808-3. View

5.
Pietromonaco S, Denslow N, OBrien T . Proteins of mammalian mitochondrial ribosomes. Biochimie. 1991; 73(6):827-35. DOI: 10.1016/0300-9084(91)90062-6. View