Structure of the Mammalian Mitochondrial Ribosome Reveals an Expanded Functional Role for Its Component Proteins
Mechanism of protein biosynthesis in mammalian mitochondria.
The Large Subunit of the Mammalian Mitochondrial Ribosome
Identification of all the protein components of the large subunit (39 S) of the mammalian mitochondrial ribosome has been achieved by carrying out proteolytic digestions of whole 39 S subunits…
The Small Subunit of the Mammalian Mitochondrial Ribosome
- E. Cavdar Koc, W. Burkhart, K. Blackburn, A. Moseley, L. Spremulli
- BiologyJournal of Biological Chemistry
- 1 June 2001
Identification of all the protein components of the small subunit (28 S) of the mammalian mitochondrial ribosome has been achieved by carrying out proteolytic digestions of whole 28 S subunits…
Interaction of Mammalian Mitochondrial Ribosomes with the Inner Membrane*
All of the products of mitochondrial protein biosynthesis in animals are hydrophobic proteins that are localized in the inner membrane. Hence, it is possible that the synthesis of these proteins…
Identification and cloning of human mitochondrial translational release factor 1 and the ribosome recycling factor.
Initiation and elongation factors in mammalian mitochondrial protein biosynthesis.
Identification of Mammalian Mitochondrial Translational Initiation Factor 3 and Examination of Its Role in Initiation Complex Formation with Natural mRNAs*
Human mitochondrial translational initiation factor 3 (IF3mt) has been identified from the human expressed sequence tag data base and the predicted mature form of IF3mt was cloned, and the protein was expressed in Escherichia coli in a His-tagged form.
Evidence for an active role of IF3mt in the initiation of translation in mammalian mitochondria.
The results suggest that IF3(mt) plays an active role in initiation of translation, and appears to lead to a factor defective in the ability to displace the large subunit of the ribosome from the 55S monosomes in an active process.
Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome
- P. S. Kaushal, Manjuli R. Sharma, R. Agrawal
- BiologyProceedings of the National Academy of Sciences
- 5 May 2014
The cryo-EM structure analysis of the small (28S) subunit (SSU) of the 55S mitoribosome is presented, finding 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.