Localization of proteins S1, S2, S16 and S23 on the surface of small subunits of rat liver ribosomes by immune electron microscopy

Lutsch, Gudrun; F, Noll; Theise, H; Enzmann, Gaby; Bielka, H

doi:10.1007/bf00273223

Cited by 49 publications

(5 citation statements)

References 20 publications

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“…The QM or L10 protein is involved in joining of the 40S with the 60S ribosomal subunit (21). Although the precise molecular function of RpS21 remains yet to be determined, this protein is associated with the surface of mammalian 40S ribosomal subunits (42) and our work shows that it is associated with native 40S ribosomal subunits and absent from polysomes, indicating a role in translation initiation. Furthermore, immunostaining and cell fractionation procedures revealed no detectable amount of RpS21 in the nucleus (data not shown), suggesting no function in the maturation or transport of the 40S ribosomal subunit from the nucleolus to the cytoplasm.…”

Section: Fig 11mentioning

confidence: 68%

Down-Regulation of RpS21, a Putative Translation Initiation Factor Interacting with P40, Produces Viable Minute Imagos and Larval Lethality with Overgrown Hematopoietic Organs and Imaginal Discs

Török

Herrmann-Horle

Kiss

et al. 1999

Molecular and Cellular Biology

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Down-regulation of the Drosophila ribosomal protein S21 gene (rpS21) causes a dominant weak Minute phenotype and recessively produces massive hyperplasia of the hematopoietic organs and moderate overgrowth of the imaginal discs during larval development. Here, we show that the S21 protein (RpS21) is bound to native 40S ribosomal subunits in a salt-labile association and is absent from polysomes, indicating that it acts as a translation initiation factor rather than as a core ribosomal protein. RpS21 can interact strongly with P40, a ribosomal peripheral protein encoded by the stubarista (sta) gene. Genetic studies reveal that P40 underexpression drastically enhances imaginal disc overgrowth in rpS21-deficient larvae, whereas viable combinations between rpS21 and sta affect the morphology of bristles, antennae, and aristae. These data demonstrate a strong interaction between components of the translation machinery and showed that their underexpression impairs the control of cell proliferation in both hematopoietic organs and imaginal discs.

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Section: Fig 11mentioning

confidence: 68%

Down-Regulation of RpS21, a Putative Translation Initiation Factor Interacting with P40, Produces Viable Minute Imagos and Larval Lethality with Overgrown Hematopoietic Organs and Imaginal Discs

Török

Herrmann-Horle

Kiss

et al. 1999

Molecular and Cellular Biology

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“…In any case, this suggests that puromycin-binding sites are located on both subunits and, moreover, not at their interface. In this context, it is interesting to note that the elongated protein S3 [which corresponds to S2 in the nomenclature of Welfle et al (1972)] has been located by immune electron microscopy in the region between the head and the body of the 40S subunit, on the side opposite to the protuberance, i.e., the side which is not in contact with the large subunit (Lutsch et al, 1979). With regard to its function, S3, as LIO, has been located at or near the P site, since it was involved in eIF-2 Met-tRNAf binding (Noll et al, 1978) and could be cross-linked to this initiation factor (Westermann et al, 1979).…”

Section: Discussionmentioning

confidence: 99%

Photoincorporation of puromycin into rat liver ribosomes and subunits

Am¹,

Dubost²,

Buisson³

et al. 1981

Biochemistry

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[3H]Puromycin was covalently incorporated into rat liver ribosomes and isolated 40S and 60S subunits on irradiation at 254 nm. A study of the concentration dependence of this photolytic incorporation suggested that it arose from specific sites on isolated subunits but also from unspecific ones in the case of ribosomes, these sites being probably located on contaminant nonribosomal proteins. Puromycin was incorporated simultaneously into ribosomal proteins and rRNAs. The results from simultaneous one-dimensional and two-dimensional gel electrophoreses showed a small distribution of label among ribosomal proteins in 60S subunits and in 80S ribosomes, L10 being the most radioactive protein. Some antibiotics, which act on the peptidyltransferase center (amicetin and gougerotin), and also tetracycline competed with this labeling. Therefore, it was concluded that puromycin interaction with protein L10 occurred most likely at a functional site. In the case of free 40S subunits, labeling distribution among proteins was much wider. The possibility that proteins S3 and perhaps S23-24, which were significantly labeled in crude ribosomes too, also belong to a specific site interacting with puromycin is discussed.

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“…The locations of 11 proteins of the 40S subunit of rat liver ribosomes [33,34,13] and the binding site of initiation factor eIF-2 [35,36] have been determined earlier by means of immuno-electron microscopy of negatively stained particles. The location of initiation factor eIF-3 in native 40S subunits was also studied using negatively stained samples [37,38].…”

Section: Locations Of 40s Ribosomal Subunit Proteins and Functional Centresmentioning

confidence: 99%

The 80S rat liver ribosome at 25 å resolution by electron cryomicroscopy and angular reconstitution

et al. 1998

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Localization of proteins S1, S2, S16 and S23 on the surface of small subunits of rat liver ribosomes by immune electron microscopy

Cited by 49 publications

References 20 publications

Down-Regulation of RpS21, a Putative Translation Initiation Factor Interacting with P40, Produces Viable Minute Imagos and Larval Lethality with Overgrown Hematopoietic Organs and Imaginal Discs

Down-Regulation of RpS21, a Putative Translation Initiation Factor Interacting with P40, Produces Viable Minute Imagos and Larval Lethality with Overgrown Hematopoietic Organs and Imaginal Discs

Photoincorporation of puromycin into rat liver ribosomes and subunits

The 80S rat liver ribosome at 25 å resolution by electron cryomicroscopy and angular reconstitution

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