Mitochondrial transport of mitoribosomal proteins, YmL8 and YmL20, in <i>Saccharomyces cerevisiae</i>

Matsushita, Yasuhiko; Isono, Katsumi

doi:10.1111/j.1432-1033.1993.tb17956.x

Cited by 12 publications

(11 citation statements)

References 41 publications

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“…YmL20 possesses a cleavable signal peptide of 18 amino acid residues [28]. The protein containing this N-terminal peptide is transported properly into mitochondria in itro [80]. In a fusion protein this signal peptide directs Chinese-hamster dehydrofolate reductase (DHFR) into mitochondria.…”

Section: Biochemical Properties Of Mrpsmentioning

confidence: 99%

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Mitochondrial ribosomal proteins (MRPs) of yeast

Graack

Wittmann‐Liebold

1998

Biochemical Journal

109

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Mitochondrial ribosomal proteins (MRPs) are the counterparts in that organelle of the cytoplasmic ribosomal proteins in the host. Although the MRPs fulfil similar functions in protein biosynthesis, they are distinct in number, features and primary structures from the latter. Most progress in the eludication of the properties of individual MRPs, and in the characterization of the corresponding genes, has been made in baker's yeast (Saccharomyces cerevisiae). To date, 50 different MRPs have been determined, although biochemical data and mutational analysis propose a total number which is substantially higher. Surprisingly, only a minority of the MRPs that have been characterized show significant sequence similarities to known ribosomal proteins from other sources, thus limiting the deduction of their functions by simple comparison of amino acid sequences. Further, individual MRPs have been characterized functionally by mutational studies, and the regulation of expression of MRP genes has been described. The interaction of the mitochondrial ribosomes with transcription factors specific for individual mitochondrial mRNAs, and the communication between mitochondria and the nucleus for the co-ordinated expression of ribosomal constituents, are other aspects of current MRP research. Although the mitochondrial translational system is still far from being described completely, the yeast MRP system serves as a model for other organisms, including that of humans.

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Section: Biochemical Properties Of Mrpsmentioning

confidence: 99%

“…In a fusion protein this signal peptide directs Chinese-hamster dehydrofolate reductase (DHFR) into mitochondria. At the same time, YmL20, lacking the N-terminal signal peptide, is also properly imported [80]. YmL8 has no cleavable signal peptide, and only the initiator methionine is cleaved off post-translationally [28].…”

Section: Biochemical Properties Of Mrpsmentioning

confidence: 99%

Mitochondrial ribosomal proteins (MRPs) of yeast

Graack

Wittmann‐Liebold

1998

Biochemical Journal

109

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“…Ribosomal proteins containing an internal targeting signal have also been found in S. cerevisiae (Matsushita & Isono, 1993).…”

Section: Targeting Signal Acquisitionmentioning

confidence: 99%

Gene Content and Gene Transfer from Mitochondria to the Nucleus During Evolution

Ueda

Kadowaki

2012

Advances in Botanical Research

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“…In the cases of the yeast MRPs without cleavable N-terminal MISPs, mitochondrial import signals can be inferred to reside in the interior of the protein sequence. YmL8, the yeast mitochondrial counterpart of mammalian MRP-L26, is transported into the mitochondria without cleavage of an N-terminal MISP (27). The signal sequence for mitochondrial import is localized internally in the middle of the protein.…”

Section: Characterization and Evolution Of Mammalian Mrps-mentioning

confidence: 99%

Mammalian Mitochondrial Ribosomal Proteins (2)

O’Brien¹,

Fiesler²,

Denslow³

et al. 1999

Journal of Biological Chemistry

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Four different classes of mammalian mitochondrial ribosomal proteins were identified and characterized. Mature proteins were purified from bovine liver and subjected to N-terminal or matrix-assisted laser-desorption mass spectroscopic amino acid sequencing after tryptic in-gel digestion and high pressure liquid chromatography separation of the resulting peptides. Peptide sequences obtained were used to virtually screen expressed sequence tag data bases from human, mouse, and rat. Consensus cDNAs were assembled in silico from various expressed sequence tag sequences identified. Deduced mammalian protein sequences were characterized and compared with ribosomal protein sequences of Escherichia coli and yeast mitochondria. Significant sequence similarities to ribosomal proteins of other sources were detected for three out of four different mammalian protein classes determined. However, the sequence conservation between mitochondrial ribosomal proteins of mammalian and yeast origin is much less than the sequence conservation between cytoplasmic ribosomal proteins of the same species. In particular, this is shown for the mammalian counterparts of the E. coli EcoL2 ribosomal protein (MRP-L14), that do not conserve the specific and functional highly important His 229 residue of E. coli and the corresponding yeast mitochondrial Rml2p.

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Mitochondrial transport of mitoribosomal proteins, YmL8 and YmL20, in Saccharomyces cerevisiae

Cited by 12 publications

References 41 publications

Mitochondrial ribosomal proteins (MRPs) of yeast

Mitochondrial ribosomal proteins (MRPs) of yeast

Gene Content and Gene Transfer from Mitochondria to the Nucleus During Evolution

Mammalian Mitochondrial Ribosomal Proteins (2)

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