ArticleBiochimica et biophysica acta2011
Contacts between mammalian mitochondrial translational initiation factor 3 and ribosomal proteins in the small subunit.
Article in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- The phenotypic spectrum ofJIMD reports · 2024Article
- Translation in Mitochondrial Ribosomes.Methods in molecular biology (Clifton, N.J.) · 2023Article
- YBEY is an essential biogenesis factor for mitochondrial ribosomes.Nucleic acids research · 2020Article
- Review
- Fidelity of translation initiation is required for coordinated respiratory complex assembly.Science advances · 2019Article
- Mitochondrial protein synthesis: figuring the fundamentals, complexities and complications, of mammalian mitochondrial translation.FEBS letters · 2014Review
- Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Review
- Protein biosynthesis in mitochondria.Biochemistry. Biokhimiia · 2013Review
- Yeast PPR proteins, watchdogs of mitochondrial gene expression.RNA biology · 2013Article
- Identification and characterization of CHCHD1, AURKAIP1, and CRIF1 as new members of the mammalian mitochondrial ribosome.Frontiers in physiology · 2013Article
- Human pentatricopeptide proteins: only a few and what do they do?RNA biology · 2013Review
- Mechanism of protein biosynthesis in mammalian mitochondria.Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Mammalian mitochondrial translational initiation factor 3 (IF3(mt)) binds to the small subunit of the ribosome displacing the large subunit during the initiation of protein biosynthesis. About half of the proteins in mitochondrial ribosomes have homologs in bacteria while the remainder are unique to the mitochondrion. To obtain information on the ribosomal proteins located near the IF3(mt) binding site, cross-linking studies were carried out followed by identification of the cross-linked proteins by mass spectrometry. IF3(mt) cross-links to mammalian mitochondrial homologs of the bacterial ribosomal proteins S5, S9, S10, and S18-2 and to unique mitochondrial ribosomal proteins MRPS29, MRPS32, MRPS36 and PTCD3 (Pet309) which has now been identified as a small subunit ribosomal protein. IF3(mt) has extensions on both the N- and C-termini compared to the bacterial factors. Cross-linking of a truncated derivative lacking these extensions gives the same hits as the full length IF3(mt) except that no cross-links were observed to MRPS36. IF3 consists of two domains separated by a flexible linker. Cross-linking of the isolated N- and C-domains was observed to a range of ribosomal proteins particularly with the C-domain carrying the linker which showed significant cross-linking to several ribosomal proteins not found in prokaryotes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.