Tag‐mediated isolation of yeast mitochondrial ribosome and mass spectrometric identification of its new components

Gan, Xiang; Kitakawa, Madoka; Yoshino, Ken‐ichi; Oshiro, Noriko; Yonezawa, Kazuyoshi; Isono, Katsumi

doi:10.1046/j.1432-1033.2002.03226.x

Cited by 59 publications

(69 citation statements)

References 43 publications

(39 reference statements)

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“…Tandem mass-spectrometry had been successfully applied to the analysis of the protein composition of ribosomes from several organelles including bovine mitochondria [32,33,[36][37][38], fungal mitochondria [39,40] and chloroplasts [41,42]. To reduce contamination by other large oligomeric complexes we have used preparations of the complexes obtained by different procedures, including monomers, spontaneously formed dimers and salt washed monomers.…”

Section: Discussionmentioning

confidence: 99%

Proteomics and electron microscopic characterization of the unusual mitochondrial ribosome-related 45S complex in Leishmania tarentolae

Maslov

Spremulli

Sharma

et al. 2007

Molecular and Biochemical Parasitology

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A novel type of ribonucleoprotein (RNP) complex has been described from the kinetoplastmitochondria of Leishmania tarentolae. The complex, termed the 45S SSU*, contains the 9S small subunit rRNA but does not contain the 12S large subunit rRNA. This complex is the most stable and abundant mitochondrial RNP complex present in Leishmania. As shown by tandem mass spectrometry, the complex contains at least 39 polypeptides with a combined molecular mass of almost 2.1 MDa. These components include several homologs of small subunit ribosomal proteins (S5, S6, S8 S9, S11, S15, S16, S17, S18, MRPS29); however, most of the polypeptides present are unique. Only a few of them show recognizable motifs, such as protein-protein (coiled-coil, Rhodanese) or protein-RNA (pentatricopeptide repeat) interaction domains. A cryo-electron microscopy examination of the 45S SSU* fraction reveals that 27% of particles represent SSU homodimers arranged in a head-to-tail orientation, while the majority of particles are clearly different and show an asymmetric bilobed morphology. Multiple classes of two-dimensional averages were derived for the asymmetrical particles, probably reflecting random orientations of the particles and difficulties in correlating these views with the known projections of ribosomal complexes. One class of the two-dimensional averages shows an SSU moiety attached to a protein mass or masses in a monosome-like appearance. The combined mass spectrometry and electron microscopy data thus indicate that the majority 45S SSU* particles represents a heterodimeric complex in which the SSU Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access

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Section: Discussionmentioning

confidence: 99%

Proteomics and electron microscopic characterization of the unusual mitochondrial ribosome-related 45S complex in Leishmania tarentolae

Maslov

Spremulli

Sharma

et al. 2007

Molecular and Biochemical Parasitology

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“…Their sedimentation coefficient (S) values vary between 50 S in Leishmania, 70 -74 S in fungi, 55 S in metazoans, and 78 S in higher plants (3)(4)(5)(6). Tandem mass spectrometry has been successfully applied to the analysis of the protein composition of ribosomes from several organelles including bovine mitochondria (5,(7)(8)(9)(10), fungal mitochondria (11,12), and chloroplasts (13,14). Mammalian ribosomes have about the same mass as bacterial ribosomes but half as much RNA and over twice as much proteins.…”

Section: Mtmentioning

confidence: 99%

Trypanosoma brucei Mitochondrial Ribosomes

Zı́ková

Panigrahi

Dalley

et al. 2008

Molecular & Cellular Proteomics

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Although eukaryotic mitochondrial (mt) ribosomes evolved from a putative prokaryotic ancestor their compositions vary considerably among organisms. We determined the protein composition of tandem affinity-purified Trypanosoma brucei mt ribosomes by mass spectrometry and identified 133 proteins of which 77 were associated with the large subunit and 56 were associated with the small subunit. Comparisons with bacterial and mammalian mt ribosomal proteins identified T. brucei mt homologs of L2-4, L7/12, L9, L11, L13-17, L20 -24, L27-30, L33, L38, L43, L46, L47, L49, L52, S5, S6, S8, S9, S11, S15-18, S29, and S34, although the degree of conservation varied widely. Sequence characteristics of some of the component proteins indicated apparent functions in rRNA modification and processing, protein assembly, and mitochondrial metabolism implying possible additional roles for these proteins. Nevertheless most of the identified proteins have no homology outside Kinetoplastida implying very low conservation and/or a divergent function in kinetoplastid mitochondria. Molecular & Cellular Proteomics 7:1286 -1296, 2008. Mt1 ribosomes appear to be structurally variable to a considerable extent from one organism to another and have undergone some major remodeling during their evolution including loss of RNA and acquisition of proteins (1, 2). Their sedimentation coefficient (S) values vary between 50 S in Leishmania, 70 -74 S in fungi, 55 S in metazoans, and 78 S in higher plants (3-6). Tandem mass spectrometry has been successfully applied to the analysis of the protein composition of ribosomes from several organelles including bovine mitochondria (5, 7-10), fungal mitochondria (11, 12), and chloroplasts (13,14). Mammalian ribosomes have about the same mass as bacterial ribosomes but half as much RNA and over twice as much proteins. Proteomics analysis of bovine mt ribosomes (9, 10) identified 78 different proteins, which include homologs of Escherichia coli ribosomal proteins and 36 additional proteins that presumably were acquired during eukaryotic evolution. Many of these new ribosomal proteins are distinct, having no closely related homologs in bacterial or eukaryotic cytoplasmic ribosomes. The estimated number of proteins within mammalian mt ribosomes has ranged from about 85 to more than 100, for yeast mitochondria it is 78 proteins, and for chloroplast mitochondria it is 49 proteins. The feature of protein richness implies that the reduced rRNA sizes are compensated by some protein components that might have been recruited to mt ribosomes during the course of evolution (15).Trypanosoma and Leishmania are protozoan parasites belonging to the order Kinetoplastida that are the causative agents of several devastating tropical diseases such as African sleeping sickness, Chagas disease, and leishmaniasis. Protein synthesis in the mitochondria of these unicellular flagellates has unusual features. The transcripts from most genes encoded in the trypanosomatid mt DNA are posttranscriptionally modified via extensive and precise ins...

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“…MRPL51 was established as a large subunit of mammalian MRPs (Gan et al 2002) and functions in the translation of genetic messages. The redistribution of mitochondria was coordinated with oocyte maturation, and lack of redistribution of mitochondria suggested incomplete cytoplasmic maturation and lower developmental competence (Krisher et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Altered expression of Armet and Mrlp51 in the oocyte, preimplantation embryo, and brain of mice following oocyte in vitro maturation but postnatal brain development and cognitive function are normal

Wang¹,

Wang²,

Fang³

et al. 2011

Reproduction

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Despite the efforts to recapitulate the follicle environment, oocytes from in vitro maturation (IVM) have poorer developmental potential than those matured in vivo and the effects on the resultant offspring are of concern. The aim of this study was to determine altered gene expression in oocytes following IVM and to evaluate the expression of the arginine rich, mutated in early stage of tumors gene (Armet) and mitochondrial ribosomal protein L51 (Mrpl51) in embryos and brains of fetal/postnatal mice and the brain development of IVM offspring. An IVM mouse model was established while oocytes matured in vivo were used as the controls. Suppressive subtractive hybridization (SSH) and RT-PCR/western blot were used to analyze the differential expression of genes/proteins between IVM and the control group. HE staining and water maze were used to assess the histological changes in brain tissue and cognition of the offspring. The rates of fertilization, cleavage, and live birth were significantly decreased in IVM group. Thirteen genes were upregulated in IVM oocytes compared with the control, including Armet and Mrpl51. The higher level of Armet in IVM oocytes was retained in brain of newborn mice, which could be related to the upregulation of activating transcription factor 6 (Atf6) and X-box binding protein 1 (Xbp1), while Mrpl51 was expressed normally in brain of postnatal mice. No significant differences were detected in brain weight, neuronal counts, and the cognition in the offspring between the two groups. The present results suggested that IVM could affect the pregnancy outcome and the Armet and Mrpl51 gene/protein expression. The change in Armet expression lasted while the change of Mrpl51 disappeared after birth. However, the brain development of the offspring seemed to be unaffected by IVM.

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Tag‐mediated isolation of yeast mitochondrial ribosome and mass spectrometric identification of its new components

Cited by 59 publications

References 43 publications

Proteomics and electron microscopic characterization of the unusual mitochondrial ribosome-related 45S complex in Leishmania tarentolae

Proteomics and electron microscopic characterization of the unusual mitochondrial ribosome-related 45S complex in Leishmania tarentolae

Trypanosoma brucei Mitochondrial Ribosomes

Altered expression of Armet and Mrlp51 in the oocyte, preimplantation embryo, and brain of mice following oocyte in vitro maturation but postnatal brain development and cognitive function are normal

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