Zinc finger-like motifs in rat ribosomal proteins S27 and S29

Chan, Yuen‐Ling; Suzuki, Katsuyuki; Olvera, Joe; Wool, Ira G.

doi:10.1093/nar/21.3.649

Cited by 79 publications

(58 citation statements)

References 39 publications

(30 reference statements)

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“…S14 gives weak rRNA footprints located in the 3Ј domain of the 16 S rRNA (27). A zinc-finger motif found in several members of the S14 family has been postulated to contribute to an interaction with rRNA (30,31). However, no zinc finger motif is present in mammalian mitochondrial S14.…”

Section: Discussionmentioning

confidence: 99%

A Proteomics Approach to the Identification of Mammalian Mitochondrial Small Subunit Ribosomal Proteins

Koc

Burkhart

Blackburn

et al. 2000

Journal of Biological Chemistry

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Mammalian mitochondrial small subunit ribosomal proteins were separated by two-dimensional polyacrylamide gel electrophoresis. The proteins in six individual spots were subjected to in-gel tryptic digestion. Peptides were separated by capillary liquid chromatography, and the sequences of selected peptides were obtained by electrospray tandem mass spectrometry. The peptide sequences obtained were used to screen human expressed sequence tag data bases, and complete consensus cDNAs were assembled. Mammalian mitochondrial small subunit ribosomal proteins from six different classes of ribosomal proteins were identified. Only two of these proteins have significant sequence similarities to ribosomal proteins from prokaryotes. These proteins correspond to Escherichia coli S10 and S14. Homologs of two human mitochondrial proteins not found in prokaryotes were observed in the genomes of Drosophila melanogaster and Caenorhabditis elegans. A homolog of one of these proteins was observed in D. melanogaster but not in C. elegans, while a homolog of the other was present in C. elegans but not in D. melanogaster. A homolog of one of the ribosomal proteins not found in prokaryotes was tentatively identified in the yeast genome. This latter protein is the first reported example of a ribosomal protein that is shared by mitochondrial ribosomes from lower and higher eukaryotes that does not have a homolog in prokaryotes.Mammalian mitochondria carry out the synthesis of 13 polypeptides that are essential for oxidative phosphorylation and, hence, for the synthesis of the majority of the ATP used by eukaryotic organisms. The protein synthesizing system of mammalian mitochondria has a number of interesting features that are not observed in the corresponding systems in prokaryotes or the cell cytoplasm (1). The ribosomes present in mammalian mitochondria are 55-60 S particles and are composed of small (28 S) and a large (39 S) subunits (2). They are characterized by a low percentage of rRNA and a compensating increase in the number of ribosomal proteins (3).Considerable progress has been made on the identification of the mitochondrial ribosomal proteins in yeast. About 50 different mitochondrial ribosomal proteins (MRPs) 1 have been identified in this organism (4). Additional protein components in yeast mitochondrial ribosomes remain to be determined. Surprisingly, less than half of the mitochondrial ribosomal proteins in yeast show significant sequence identities to the ribosomal proteins of other systems (4). Analysis of the protein composition of mammalian mitochondrial ribosomes indicates that they have more proteins than observed in bacterial ribosomes (5). Limited information is available on the identities of these proteins and on their relationships to bacterial ribosomal proteins. Recently, 18 proteins of the large subunit and 5 proteins of the small subunit of the mammalian mitochondrial ribosome have been characterized primarily by peptide sequencing coupled to the extensive use of the EST data bases to deduce the full-length c...

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Section: Discussionmentioning

confidence: 99%

A Proteomics Approach to the Identification of Mammalian Mitochondrial Small Subunit Ribosomal Proteins

Koc

Burkhart

Blackburn

et al. 2000

Journal of Biological Chemistry

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“…RPS27, also called metallopanstimulin-1 (MPS-1), was first identified as a growth factor inducible gene which encodes a 9.5 kDa protein of 84 amino acids with a zinc-finger-like motif (Chan et al, 1993;FernandezPol et al, 1993;Wong et al, 1993). RPS27/MPS-1 is a nuclear protein and overexpressed in large quantities in various proliferating tissues (Fernandez-Pol et al, 1994) and in multiple human cancers, including carcinomas of colon (Ganger et al, 1997;Wong et al, 1993), prostate , breast (Atsuta et al, 2002), liver (Ganger et al, 2001), and head and neck .…”

Section: Rps27l Induction By P53 H He and Y Sunmentioning

confidence: 99%

Ribosomal protein S27L is a direct p53 target that regulates apoptosis

Sun

2006

Oncogene

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“…They have high codon biases, 0.745 and 0.510, respectively, as expected for yeast ribosomal protein genes. The predicted proteins have a zinc finger-like motif of the C2-C2 type as do many other ribosomal proteins from eukaryotes, archaebacteria, eubacteria, and mitochondria (9).…”

Section: Figmentioning

confidence: 99%

Functional Analysis of Rrp7p, an Essential Yeast Protein Involved in Pre-rRNA Processing and Ribosome Assembly

Baudin-Baillieu

Tollervey

Cullin

et al. 1997

Molecular and Cellular Biology

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During the functional analysis of open reading frames (ORFs) identified during the sequencing of chromosome III of Saccharomyces cerevisiae, the previously uncharacterized ORF YCL031C (now designated RRP7) was deleted. RRP7 is essential for cell viability, and a conditional null allele was therefore constructed, by placing its expression under the control of a regulated GAL promoter. Genetic depletion of Rrp7p inhibited the prerRNA processing steps that lead to the production of the 20S pre-rRNA, resulting in reduced synthesis of the 18S rRNA and a reduced ratio of 40S to 60S ribosomal subunits. A screen for multicopy suppressors of the lethality of the GAL::rrp7 allele isolated the two genes encoding a previously unidentified ribosomal protein (r-protein) that is highly homologous to the rat r-protein S27. When present in multiple copies, either gene can suppress the lethality of an RRP7 deletion mutation and can partially restore the ribosomal subunit ratio in Rrp7p-depleted cells. Deletion of both r-protein genes is lethal; deletion of either single gene has an effect on pre-rRNA processing similar to that of Rrp7p depletion. We believe that Rrp7p is required for correct assembly of rpS27 into the preribosomal particle, with the inhibition of pre-rRNA processing appearing as a consequence of this defect.The biosynthesis of eukaryotic ribosome is a complex process that occurs in a subnuclear organelle: the nucleolus (for reviews, see references 15 and 32). In the yeast Saccharomyces cerevisiae, between 100 and 200 copies of the rRNA gene (rDNA) are present on chromosome XII. Each repeated transcription unit is transcribed by RNA polymerase I into a 7-kb, 35S primary transcript that contains the 18S, 5.8S, and 25S rRNA sequences separated by internal transcribed spacers (ITS) and flanked by external transcribed spacers (ETS). The 35S transcript undergoes a complex series of cleavages and trimming reactions that remove the spacer regions, releasing the three mature rRNA species. The early steps in pre-rRNA processing, cleavage at sites A 0 , A 1 , and A 2 , separate the 20S pre-rRNA from the 27SA 2 pre-rRNA. 20S pre-rRNA is the precursor to the 18S rRNA which is incorporated into the 40S ribosomal subunit, while 27SA 2 contains the 5.8S and 25S rRNAs which are destined to form the 60S subunit. In many cases, mutations affect only the processing reactions on either the pathway of 18S synthesis or the pathway of 5.8S-25S synthesis (38).During the pre-rRNA processing events, many of the approximately 80 ribosomal proteins assemble onto the rRNA, but little detailed knowledge is available on the assembly pathway in eukaryotes. Mutations in r-protein genes lead to the inhibition of synthesis of the subunit of which they are components, presumably as a consequence of defects in subunit assembly (40). Ribosomal proteins L1 and rp59 are necessary for production of the 60S and the 40S subunits, respectively (11, 23), as well as the UBI1 to UBI3 genes that encode ribosomal proteins (12), while a mutation in the ribosomal ...

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Zinc finger-like motifs in rat ribosomal proteins S27 and S29

Cited by 79 publications

References 39 publications

A Proteomics Approach to the Identification of Mammalian Mitochondrial Small Subunit Ribosomal Proteins

A Proteomics Approach to the Identification of Mammalian Mitochondrial Small Subunit Ribosomal Proteins

Ribosomal protein S27L is a direct p53 target that regulates apoptosis

Functional Analysis of Rrp7p, an Essential Yeast Protein Involved in Pre-rRNA Processing and Ribosome Assembly

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