Structure of the yeast mitochondrial large ribosomal subunitStructure of the yeast mitochondrial large ribosomal subunit

Structural highlights

3j6b is a 40 chain structure with sequence from Saccharomyces cerevisiae. This structure supersedes and combines the now removed PDB entries 1vw3 and 1vw4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
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Function

[RTC6_YEAST] Probable component of the mitochondrial large ribosomal subunit involved in ribosome biogenesis and translation. May be involved in a process influencing telomere capping.[1] [2] [3] [MHR1_YEAST] Transcription factor involved in regulation of RNA polymerase II-dependent transcription. Also involved in regulation of mitochondrial DNA recombination, maintenance and repair, and generation of homoplasmic cells.[4] [5] [6] [7] [8] [9] [10] [RM36_YEAST] Involved in mitochondrial translation. Overexpression suppresses mutations in the COX2 leader peptide-encoding and initiation codon regions.[11] [12] [IMG1_YEAST] Essential for respiration.[13] [RM06_YEAST] Indispensable for mitochondrial function.

Publication Abstract from PubMed

Mitochondria have specialized ribosomes that have diverged from their bacterial and cytoplasmic counterparts. We have solved the structure of the yeast mitoribosomal large subunit using single-particle cryo-electron microscopy. The resolution of 3.2 angstroms enabled a nearly complete atomic model to be built de novo and refined, including 39 proteins, 13 of which are unique to mitochondria, as well as expansion segments of mitoribosomal RNA. The structure reveals a new exit tunnel path and architecture, unique elements of the E site, and a putative membrane docking site.

Structure of the yeast mitochondrial large ribosomal subunit.,Amunts A, Brown A, Bai XC, Llacer JL, Hussain T, Emsley P, Long F, Murshudov G, Scheres SH, Ramakrishnan V Science. 2014 Mar 28;343(6178):1485-9. doi: 10.1126/science.1249410. PMID:24675956[14]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Andrade MA, Daruvar A, Casari G, Schneider R, Termier M, Sander C. Characterization of new proteins found by analysis of short open reading frames from the full yeast genome. Yeast. 1997 Nov;13(14):1363-74. PMID:9392081 doi:<1363::AID-YEA182>3.0.CO;2-8 http://dx.doi.org/10.1002/(SICI)1097-0061(199711)13:14<1363::AID-YEA182>3.0.CO;2-8
  2. Addinall SG, Downey M, Yu M, Zubko MK, Dewar J, Leake A, Hallinan J, Shaw O, James K, Wilkinson DJ, Wipat A, Durocher D, Lydall D. A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied cellular processes influencing telomere capping in Saccharomyces cerevisiae. Genetics. 2008 Dec;180(4):2251-66. Epub 2008 Oct 9. PMID:18845848 doi:http://dx.doi.org/genetics.108.092577
  3. Alamgir M, Erukova V, Jessulat M, Azizi A, Golshani A. Chemical-genetic profile analysis of five inhibitory compounds in yeast. BMC Chem Biol. 2010 Aug 6;10:6. doi: 10.1186/1472-6769-10-6. PMID:20691087 doi:http://dx.doi.org/10.1186/1472-6769-10-6
  4. Ling F, Morioka H, Ohtsuka E, Shibata T. A role for MHR1, a gene required for mitochondrial genetic recombination, in the repair of damage spontaneously introduced in yeast mtDNA. Nucleic Acids Res. 2000 Dec 15;28(24):4956-63. PMID:11121487
  5. Emili A, Kobayashi R, Ingles CJ. A novel yeast protein influencing the response of RNA polymerase II to transcriptional activators. Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11122-7. PMID:9736700
  6. Ling F, Makishima F, Morishima N, Shibata T. A nuclear mutation defective in mitochondrial recombination in yeast. EMBO J. 1995 Aug 15;14(16):4090-101. PMID:7664749
  7. Ling F, Shibata T. Recombination-dependent mtDNA partitioning: in vivo role of Mhr1p to promote pairing of homologous DNA. EMBO J. 2002 Sep 2;21(17):4730-40. PMID:12198175
  8. Traven A, Staresincic L, Arneric M, Sopta M. The yeast protein Xtc1 functions as a direct transcriptional repressor. Nucleic Acids Res. 2002 Jun 1;30(11):2358-64. PMID:12034822
  9. Ling F, Shibata T. Mhr1p-dependent concatemeric mitochondrial DNA formation for generating yeast mitochondrial homoplasmic cells. Mol Biol Cell. 2004 Jan;15(1):310-22. Epub 2003 Oct 17. PMID:14565971 doi:http://dx.doi.org/10.1091/mbc.E03-07-0508
  10. Mookerjee SA, Sia EA. Overlapping contributions of Msh1p and putative recombination proteins Cce1p, Din7p, and Mhr1p in large-scale recombination and genome sorting events in the mitochondrial genome of Saccharomyces cerevisiae. Mutat Res. 2006 Mar 20;595(1-2):91-106. PMID:16337661 doi:http://dx.doi.org/S0027-5107(05)00465-3
  11. Bonnefoy N, Bsat N, Fox TD. Mitochondrial translation of Saccharomyces cerevisiae COX2 mRNA is controlled by the nucleotide sequence specifying the pre-Cox2p leader peptide. Mol Cell Biol. 2001 Apr;21(7):2359-72. PMID:11259585 doi:http://dx.doi.org/10.1128/MCB.21.7.2359-2372.2001
  12. Williams EH, Perez-Martinez X, Fox TD. MrpL36p, a highly diverged L31 ribosomal protein homolog with additional functional domains in Saccharomyces cerevisiae mitochondria. Genetics. 2004 May;167(1):65-75. PMID:15166137
  13. Coppee JY, Rieger KJ, Kaniak A, di Rago JP, Groudinsky O, Slonimski PP. PetCR46, a gene which is essential for respiration and integrity of the mitochondrial genome. Yeast. 1996 May;12(6):577-82. PMID:8771712 doi:<577::AID-YEA950>3.0.CO;2-2 http://dx.doi.org/10.1002/(SICI)1097-0061(199605)12:6<577::AID-YEA950>3.0.CO;2-2
  14. Amunts A, Brown A, Bai XC, Llacer JL, Hussain T, Emsley P, Long F, Murshudov G, Scheres SH, Ramakrishnan V. Structure of the yeast mitochondrial large ribosomal subunit. Science. 2014 Mar 28;343(6178):1485-9. doi: 10.1126/science.1249410. PMID:24675956 doi:http://dx.doi.org/10.1126/science.1249410

3j6b, resolution 3.20Å

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