Ribosomal protein S18e as a putative molecular staple for the 18S rRNA 3′-major domain core

ABSTRACT Production of ribosomal protein S14 in Saccharomyces cerevisiae is coordinated with the rate of ribosome assembly by a feedback mechanism that represses expression of RPS14B. Three-hybrid assays in vivo and filter binding assays in vitro demonstrate that rpS14 directly binds to an RNA stem-loop structure inRPS14B pre-mRNA that is necessary for RPS14Bregulation. Moreover, rpS14 binds to a conserved helix in 18S rRNA with approximately five- to sixfold-greater affinity. These results support the model that RPS14B regulation is mediated by direct binding of rpS14 either to its pre-mRNA or to rRNA. Investigation of these interactions with the three-hybrid system reveals two regions of rpS14 that are involved in RNA recognition. D52G and E55G mutations in rpS14 alter the specificity of rpS14 for RNA, as indicated by increased affinity for RPS14B RNA but reduced affinity for the rRNA target. Deletion of the C terminus of rpS14, where multiple antibiotic resistance mutations map, prevents binding of rpS14 to RNA and production of functional 40S subunits. The emetine-resistant protein, rpS14-EmRR, which contains two mutations near the C terminus of rpS14, does not bind either RNA target in the three-hybrid or in vitro assays. This is the first direct demonstration that an antibiotic resistance mutation alters binding of an r protein to rRNA and is consistent with the hypothesis that antibiotic resistance mutations can result from local alterations in rRNA structure.

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Binding of human ribosomal protein S16 with 18S rRNA fragment 1203–1236/1521–1698

Molecular Biology ◽

10.1134/s0026893307060106 ◽

2007 ◽

Vol 41 (6) ◽

pp. 932-938 ◽

Cited By ~ 6

Author(s):

D. D. Yanshina ◽

A. A. Malygin ◽

G. G. Karpova

Keyword(s):

Ribosomal Protein ◽

18S Rrna ◽

Human Ribosomal Protein ◽

Human Ribosomal Protein S16

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Description of the bark beetle associated nematodes Micoletzkya masseyi n. sp. and M. japonica n. sp. (Nematoda: Diplogastridae)

Nematology ◽

10.1163/15685411-00002672 ◽

2013 ◽

Vol 15 (2) ◽

pp. 213-231 ◽

Cited By ~ 7

Author(s):

Vladislav Susoy ◽

Natsumi Kanzaki ◽

Matthias Herrmann

Keyword(s):

New Species ◽

Ribosomal Protein ◽

Bark Beetles ◽

18S Rrna ◽

Molecular Data ◽

Biological Data ◽

28S Rrna ◽

Ribosomal Protein Genes ◽

Male Tail ◽

Female Tail

Micoletzkya masseyi n. sp. and M. japonica n. sp. from bark beetles Orthotomicus caelatus and Dryocoetes uniseriatus, respectively, are described based on morphology and molecular data. Both species are gonochoristic and can be cultured monoxenically on bacteria. Micoletzkya masseyi n. sp. is differentiated from other species of the genus by a very short male tail, P6-P8 genital papillae arranged in a triangle and with P7 being closer to P8 than to P6, and a conoid female tail to a sharp terminus. Micoletzkya japonica n. sp. is distinct from other Micoletzkya species by the arrangement of its male papillae such that P6 and P7 are close to each other and P8 is positioned apart from them, a conoid male tail with a spicate terminus, and a small gubernaculum (ca 11 μm in length). Phylogeny of the genus was inferred using nucleotide sequences of 18S rRNA, 28S rRNA, COI, and two ribosomal protein genes. Biological data for the new species are presented and the associations between Micoletzkya species and bark beetles are discussed.

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Mg2+ ions affect structure of central domain of 18S rRNA near ribosomal protein S13 binding site

Molecular Biology ◽

10.1134/s0026893312060088 ◽

2013 ◽

Vol 47 (1) ◽

pp. 140-148 ◽

Cited By ~ 2

Author(s):

A. V. Ivanov ◽

A. A. Malygin ◽

G. G. Karpova

Keyword(s):

Ribosomal Protein ◽

Binding Site ◽

18S Rrna ◽

Central Domain ◽

Ribosomal Protein S13

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Binding of the human ribosomal protein S13 to the central domain of 18S rRNA

Molecular Biology ◽

10.1134/s0026893311050074 ◽

2011 ◽

Vol 45 (6) ◽

pp. 959-966 ◽

Cited By ~ 3

Author(s):

A. V. Ivanov ◽

A. A. Malygin ◽

G. G. Karpova

Keyword(s):

Ribosomal Protein ◽

18S Rrna ◽

Central Domain ◽

Human Ribosomal Protein ◽

Ribosomal Protein S13 ◽

Human Ribosomal Protein S13

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Human 28s rRNA 5’ terminal derived small RNA inhibits ribosomal protein mRNA levels

10.1101/618520 ◽

2019 ◽

Cited By ~ 1

Author(s):

Shuai Li

Keyword(s):

Gene Expression ◽

Ribosomal Protein ◽

Small Rna ◽

18S Rrna ◽

High Throughput Sequencing ◽

Gene Expression Omnibus ◽

28S Rrna ◽

Mrna Levels ◽

Human Tissues ◽

Sequencing Studies

AbstractRecent small RNA (sRNA) high-throughput sequencing studies reveal ribosomal RNAs (rRNAs) as major resources of sRNA. By reanalyzing sRNA sequencing datasets from Gene Expression Omnibus (GEO), we identify 28s rRNA 5’ terminal derived sRNA (named 28s5-rtsRNA) as the most abundant rRNA-derived sRNAs. These 28s5-rtsRNAs show a length dynamics with identical 5’ end and different 3’ end. Through exploring sRNA sequencing datasets of different human tissues, 28s5-rtsRNA is found to be highly expressed in bladder, macrophage and skin. We also show 28s5-rtsRNA is independent of microRNA biogenesis pathway and not associated with Argonaut proteins. Overexpression of 28s5-rtsRNA could alter the 28s/18s rRNA ratio and decrease multiple ribosomal protein mRNA levels. Our results reveal that 28s5-rtsRNA serves as a key regulator in ribosomal protein expression.

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