Ribosomal protein L25 from<i>Trypanosoma brucei</i>: phytogeny and molecular co-evolution of an rRNA-binding protein and its rRNA binding site

Metzenberg, Stan; Joblet, Christine; Verspieren, P.; Agabian, Nina

doi:10.1093/nar/21.21.4936

Cited by 20 publications

(14 citation statements)

References 38 publications

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“…Although all known eukaryotic members of this protein family have an N-terminal extension of variable length, harboring the NLS (7,21,31), the proposed D. melanogaster L23a homologue (and several other L23a homologues discussed in this paper) is even more structurally divergent in the N-terminal region. Fruit fly L23a carries an extra domain of approximately 135 amino acids (aa) with similarity to histone H1 (32), extending its overall size to 277 aa (33; accession NP_523886) compared to the yeast L25 protein of 142 aa (34; accession P04456; Figure 1 and Table 1).…”

Section: Introductionmentioning

confidence: 93%

Functional conservation between structurally diverse ribosomal proteins from Drosophila melanogaster and Saccharomyces cerevisiae: fly L23a can substitute for yeast L25 in ribosome assembly and function

Ross

Patel

Mendelson

et al. 2007

Nucleic Acids Research

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The proposed Drosophila melanogaster L23a ribosomal protein features a conserved C-terminal amino acid signature characteristic of other L23a family members and a unique N-terminal extension [Koyama et al. (Poly(ADP-ribose) polymerase interacts with novel Drosophila ribosomal proteins, L22 and l23a, with unique histone-like amino-terminal extensions. Gene 1999; 226: 339–345)], absent from Saccharomyces cerevisiae L25 that nearly doubles the size of fly L23a. The ability of fly L23a to replace the role of yeast L25 in ribosome biogenesis was determined by creating a yeast strain carrying an L25 chromosomal gene disruption and a plasmid-encoded FLAG-tagged L23a gene. Though affected by a reduced growth rate, the strain is dependent on fly L23a-FLAG function for survival and growth, demonstrating functional compatibility between the fly and yeast proteins. Pulse-chase experiments reveal a delay in rRNA processing kinetics, most notably at a late cleavage step that converts precursor 27S rRNA into mature 25S rRNA, likely contributing to the strain's slower growth pattern. Yet, given the essential requirement for L23(a)/L25 in ribosome biogenesis, there is a remarkable tolerance for accommodating the fly L23a N-terminal extension within the structure of the yeast ribosome. A search of available databases shows that the unique N-terminal extension is shared by multiple insect lineages. An evolutionary perspective on L23a structure and function within insect lineages is discussed.

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Section: Introductionmentioning

confidence: 93%

Functional conservation between structurally diverse ribosomal proteins from Drosophila melanogaster and Saccharomyces cerevisiae: fly L23a can substitute for yeast L25 in ribosome assembly and function

Ross

Patel

Mendelson

et al. 2007

Nucleic Acids Research

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“…Functional annotation of all contigs was based on best a relationship between ribosomal protein L23a (L25 in yeast) and hidden break processing because most organisms with a central hidden break harbor a flexible histone H1-like N-terminal extension (NTE) in L23a; the NTE of L23a, although its structure cannot be visualized, appears to be located adjacent to the central hidden break site (Fig. S4) [26][27][28][29]. S. marmorata L23a (contig_05690 in our transcripts) contains the NTE of approximately 180 amino acids (full-length is 326 amino acids) with relatively high homology to corresponding part in B. mori and D. melanogaster, but not in H. sapiens (Fig.…”

Section: Next-generation Sequencing Transcriptome Analysis Of Silk Glmentioning

confidence: 99%

Characterization of silk gland ribosomes from a bivoltine caddisfly, Stenopsyche marmorata : translational suppression of a silk protein in cold conditions

Nomura

Ito

Kanamori

et al. 2016

Biochemical and Biophysical Research Communications

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“…Subunit biogenesis is an ordered process that involves specific interactions of the proteins with both the RNA and other ribosomal proteins. L23 is a primary binding protein that binds and protects from RNase action a terminal loop and part of an internal loop in 23S RNA domain III (3); this binding motif is phylogenetically conserved in large subunit rRNA and is required for L23 binding to eubacterial and chloroplast RNA and for the binding of its eukaryotic homologue, L25 (39,40). Inactivation of the yeast genes for either the mitochondrial or cytoplasmic ribosome homologues of L23 is lethal (41,42), suggesting a central role in the ribosome.…”

Section: Reconstitution Of 50 S Subunits With [ 3 H]dnp-l23-50mentioning

confidence: 99%

Incorporation of Dinitrophenyl Protein L23 into Totally Reconstituted Escherichia coli 50 S Ribosomal Subunits and Its Localization at Two Sites by Immune Electron Microscopy

Montesano-Roditis¹,

Glitz²,

Perrault³

et al. 1997

Journal of Biological Chemistry

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Escherichia coli ribosomal protein L23 was derivatized with [ 3 H]2,4-dinitrofluorobenzene both at the N terminus and at internal lysines. Dinitrophenyl-L23 (DNP-L23) was taken up into 50 S subunits from a reconstitution mixture containing rRNA and total 50 S protein depleted in L23. Unmodified L23 competed with DNP-L23 for uptake, indicating that each protein form bound in an identical or similar position within the subunit. Modified L23, incorporated at a level of 0.7 or 0.4 DNP groups per 50 S, was localized by electron microscopy of subunits complexed with antibodies to dinitrophenol. Antibodies were seen at two major sites with almost equal frequency. One site is beside the central protuberance, in a region previously identified as the peptidyltransferase center. The second location is at the base of the subunit, in the area of the exit site from which the growing peptide leaves the ribosome. Models derived from image reconstruction show hollows or canyons in the subunit and a tunnel that links the transferase and exit sites. Our results indicate that L23 is at the subunit interior, with separate elements of the protein at the subunit surface at or near both ends of this tunnel.Determination of the positions of proteins within the 30 S and 50 S ribosomal subunits has been a major goal of studies directed toward the elucidation of the structure and function of the Escherichia coli ribosome. The technique of immune electron microscopy (IEM), 1 the visualization in electron micrographs of complexes formed between ribosomal subunits and specific antibodies, has been especially useful for this purpose (1, 2). However, in the case of protein L23, application of IEM has yielded controversial results. The object of the present work is to resolve this controversy.E. coli ribosomal protein L23 is a primary binding protein; it interacts directly with ribosomal RNA (3) and plays a significant role in the assembly of the large ribosomal subunit (4). The protein has been linked to the ribosomal peptidyltransferase center in several ways. First, photoaffinity labeling of 70 S ribosomes with either puromycin (5-7) or p-azidopuromycin (8, 9), each of which inhibits protein synthesis by acting as a peptide acceptor in the transferase reaction, led to photoincorporation into L23 as the major site of protein labeling. Second, antibodies recognizing the N 6 ,N 6 -dimethyladenosine moiety of puromycin bound to labeled 50 S subunits in a region generally agreed to include the peptidyltransferase center, i.e. between the central protuberance and the site of protein L1, near the 30 S:50 S interface (10, 11). Third, chemical cross-linking and related studies showed L23 to neighbor other proteins (L2, L15, L16, and L27) that have been placed at or near the peptidyltransferase center (12). Finally, although peptidyltransferase activity is not altered in reconstituted 50 S subunits either lacking L23 or including puromycin-modified L23 in place of L23, the latter do show reduced aminoacyl-tRNA binding (6), which suggests proximity to t...

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Ribosomal protein L25 fromTrypanosoma brucei: phytogeny and molecular co-evolution of an rRNA-binding protein and its rRNA binding site

Cited by 20 publications

References 38 publications

Functional conservation between structurally diverse ribosomal proteins from Drosophila melanogaster and Saccharomyces cerevisiae: fly L23a can substitute for yeast L25 in ribosome assembly and function

Functional conservation between structurally diverse ribosomal proteins from Drosophila melanogaster and Saccharomyces cerevisiae: fly L23a can substitute for yeast L25 in ribosome assembly and function

Characterization of silk gland ribosomes from a bivoltine caddisfly, Stenopsyche marmorata : translational suppression of a silk protein in cold conditions

Incorporation of Dinitrophenyl Protein L23 into Totally Reconstituted Escherichia coli 50 S Ribosomal Subunits and Its Localization at Two Sites by Immune Electron Microscopy

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