Identification of the yeast nuclear gene for the mitochondrial homologue of bacterial ribosomal protein L16

Pan, Chin Chen; Mason, Thomas L.

doi:10.1093/nar/23.18.3673

Cited by 16 publications

(12 citation statements)

References 39 publications

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“…We named it YmL47 and searched for the gene that could code for the two sequences. We consequently found the gene for YmL47 which was in fact identical to the gene encoding protein Rmll6p reported by Pan and Mason [15]. A nucleotide sequence capable of encoding the N-terminal 38 residues of protein YniL1.5 was found to be present between ORFs YLR312c and YLR313c on chromosome XI1 (Table 3).…”

Section: Resultssupporting

confidence: 76%

Identification and Characterization of the Genes for Mitochondrial Ribosomal Proteins of Saccharomyces Cerevisiae

Kitakawa

Graack

Grohmann

et al. 1997

European Journal of Biochemistry

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We have purified 13 large subunit proteins of the mitochondrial ribosome of the yeast Saccharomyces cerevisiae and determined their partial amino acid sequences. To elucidate the structure and function of these proteins, we searched for their genes by comparing our sequence data with those deduced from the genomic nucleotide sequence data of S. cerevisiae and analyzed them. In addition, we searched for the genes encoding proteins whose N-terminal amino acid sequences we have reported previously [Grohmann, L., Graack, H.-R., Kruft, V., Choli, T., Goldschmidt-Reisin, S. & Kitakawa, M. (1991) FEBS Lett. 284, 51 -561. Thus, we were able to identify and characterize 12 new genes for large subunit proteins of the yeast mitochondrial ribosome. Furthermore, we determined the N-terminal amino acid sequences of seven small subunit proteins and subsequently identified the genes for five of them, three of which were found to be new. [ 5 , 6 ] . About a half of the yeast mitoribosoma1 proteins characterized so far show a high degree of similarity to eubacterial ribosomal proteins, supporting the notion that mitochondria indeed originate from eubacteria-like organisms. However, the other half of the mitoribosomal proteins show no apparent similarity to any known ribosomal proteins of eubacterial or eukaryotic (cytoplasmic) origin. Considering the fact that mitoribosomes appear to contain more proteins than Escherichiu coli ribosomes [I], those proteins which are not similar to any known ribosomal proteins might have been recruited during the course of evolution from other sources unrelated to ribosomes. There are nonetheless many E. coli ribosomal proteins whose homologues have not yet been identified in the yeast mitoribosome: these proteins include L7L12 and L2.5 which have been shown to be present in all eubacterial ribosomes studied so far and are implicated as being functionally important. Therefore, from an evolutionary point of view, it is of great interest to investigate how many proteins are present in the mitoribosome of S. cerevisiae and with which eubacterial ribosomal proteins they have evolutionary relations. Now that the nucleotide sequence of the entire genome of S.cerevisiae has been determined, it is possible to identify the genes encoding mitoribosomal proteins by computer search if the amino acid sequences of their peptides, even as short as several residues, are known. During the course of our amino acid sequence analysis of yeast mitoribosomal proteins, we obtained fragmentary sequence data for many large subunit and several small subunit proteins. Therefore, we used the data to search for likely yeast genes encoding mitoribosomal proteins as will be described below. MATERIALS AND METHODSMitochondria were prepared from cells of S. cerevisiae strain 07173 (da; wild type), and mitoribosomal proteins were extracted from the small and large subunits separated by sucrose gradient centrifugation as described [3].About . 5 A,,, units of TP50 (total large subunit proteins), dialyzed against 5 % acetic acid, we...

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Section: Resultssupporting

confidence: 76%

Identification and Characterization of the Genes for Mitochondrial Ribosomal Proteins of Saccharomyces Cerevisiae

Kitakawa

Graack

Grohmann

et al. 1997

European Journal of Biochemistry

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“…These genes include those encoding mitochondrial ribosomal proteins; assembly factors; components of the respiratory complexes; proteins required for import, stabilization, and processing of cytoplasmically synthesized mitochondrial proteins; and known and putative members of the family of mitochondrial carrier proteins. Although it has been previously reported that mRNA levels for the mitochondrial ribosomal proteins Mrp13, Mrp49, and Rml2 are induced in rho 0 cells (27,40,41), other genes such as MRP2, MRP7, MRPL16, and CYC1 had been reported to not change (26,(42)(43)(44). In our study, although all of those particular genes showed increased expression, MRPL33 and MRP20, reported to be induced in rho 0 cells (40,45), were…”

Section: Transcription Of Nuclear Genes Involved In Mitochondrial Biomentioning

confidence: 97%

Interorganellar Communication

Traven

Wong

et al. 2001

Journal of Biological Chemistry

193

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“…Three proteins, L2, L16, and L27, are particularly interesting because crosslinking experiments consistently show that they make contacts with antibiotics that inhibit peptidyl transferase and with the 3' ends of tRNA bound in the A or P sites (for review, see [10]). The identities of the nuclear genes for the yeast mitochondrial r-proteins related to bacterial L2, L16, and L27 have been confirmed by gene disruption and each protein is essential for ribosomal function in vivo [13][14][15] …”

Section: Proteins Implicated In the Ptc Of The Yeast Mitochondrial Rimentioning

confidence: 96%

Molecular genetics of the peptidyl transferase center and the unusual Var1 protein in yeast mitochondrial ribosomes

et al. 1996

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Mitochondria possess their own ribosomes responsible for the synthesis of a small number of proteins encoded by the mitochondrial genome. In yeast, Saccharomyces cerevisiae, the two ribosomal RNAs and a single ribosomal protein, Var1, are products of mitochondrial genes, and the remaining approximately 80 ribosomal proteins are encoded in the nucleus. The mitochondrial translation system is dispensable in yeast, providing an excellent experimental model for the molecular genetic analysis of the fundamental properties of ribosomes in general as well as adaptations required for the specialized role of ribosomes in mitochondria. Recent studies of the peptidyl transferase center, one of the most highly conserved functional centers of the ribosome, and the Var1 protein, an unusual yet essential protein in the small ribosomal subunit, have provided new insight into conserved and divergent features of the mitochondrial ribosome.

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Identification of the yeast nuclear gene for the mitochondrial homologue of bacterial ribosomal protein L16

Abstract: ABSTRACT

Cited by 16 publications

References 39 publications

Identification and Characterization of the Genes for Mitochondrial Ribosomal Proteins of Saccharomyces Cerevisiae

Identification and Characterization of the Genes for Mitochondrial Ribosomal Proteins of Saccharomyces Cerevisiae

Interorganellar Communication

Molecular genetics of the peptidyl transferase center and the unusual Var1 protein in yeast mitochondrial ribosomes

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