An RNA core in the 30S ribosomal subunit of and its structural and functional significance

Garrett, Roger A.; Ungewickell, Ernst; Newberry, Veronica; Hunter, Jack B.; Wagner, Rolf

doi:10.1016/0309-1651(77)90086-8

Cited by 31 publications

(6 citation statements)

References 45 publications

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“…In this respect, it is comparable with the RNA binding site of protein S4 which constitutes a resistant region at the 5'-end of 16S RNA (32). In contrast, L18 which is released from the RNA during digestion may have a complex and more extensive interaction with the 5S RNA tertiary structure.…”

Section: Resultsmentioning

confidence: 94%

A ribonuclease-resistant region of 5S RNA and its relation to the RNA binding sites of proteins L18 and L25

Douthwaite¹,

Garrett²,

Wagner³

et al. 1979

Nucl Acids Res

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An RNA fragment, constituting three subfragments of nucleotide sequences 1-11, 69-87 and 89-120, is the most ribonucleaseresistant part of the native 5S RNA of Escherichia coli, at 0°C. A smaller fragment of nucleotide sequence 69-87 and 90-110 is ribonuclease-resistant at 250.Degradation of the L25-5S RNA complex with ribonuclease A or T2 yielded RNA fragments similar to those of the free 5S RNA at 0°C and 25°C; moreover L25 remained strongly bound to both RNA fragments and also produced some opening of the RNA structure in at least two positions.Protein L18 initially protected most of the 5S RNA against ribonuclease digestion, at 0°C, but was then gradually released prior to the formation of the larger RNA fragment. It cannot be concluded, therefore, as it was earlier (Gray et al., 1973), that this RNA fragment contains the primary binding site of L18.

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Section: Resultsmentioning

confidence: 94%

A ribonuclease-resistant region of 5S RNA and its relation to the RNA binding sites of proteins L18 and L25

Douthwaite¹,

Garrett²,

Wagner³

et al. 1979

Nucl Acids Res

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“…Since both RNAs contain domain II and the major difference between them is the presence or absence of domain I, the results indicate that domain I interacts with domain II in such a way that the two domains together become more compact than domain II by itself. This phenomenon may be relevant to the notion that domain I acts as an organizing nucleus which, by interacting with other domains of the 16 S RNA (which are synthesized later), plays a major role in determining the ultimate structure of the 30 S ribosome (35).…”

Section: Discussionmentioning

confidence: 94%

A ribonucleoprotein fragment of the 30 S ribosome ofE. colicontaining two contiguous domains of the 16 S RNA

et al. 1982

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Ribonucleoprotein fragments of the 30 S ribosome of E. coli have been prepared by limited ribonuclease digestion and mild heating of the ribosome in a constant ionic environment. One such fragment has been described previously. A second electrophoretically homogeneous fragment has now been isolated and its RNA and protein moieties have been characterized. It contains the 5' half of the 16 S RNA, encompassing domains I and II except for the extreme 5' terminus and several small gaps. Seven proteins are present: S4, S5, S6, S8, S12, S15 and S20. The RNA binding sites of five of these proteins are known, and all are RNA sequences that are present in the fragment. Published neutron scattering and immuno-electron microscopic data indicate that six of the proteins are clustered together in a cross sectional slice through the center of the subunit. After deproteinization, the RNA moiety gives two bands in gel electrophoresis, one containing domains I and II and the other, essentially only domain II. The former, although larger, migrates faster in gel electrophoresis, indicating that RNA domains I and II interact with each other in such a way as to become more compact than domain II by itself.

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“…Eukaryotic ribosomes are more complex in terms of both their rRNA and protein constituents. In bacteria the 30S small subunit contains a 16S rRNA measuring 1.5 kb, while the eukaryote equivalent (40S) RNA of over 1.9 kb (Chaker‐Margot, 2018; Garrett, Ungewickell, Newberry, Hunter, & Wagner, 1977; Melnikov et al, 2012; Moore, 1988; Rajendhran & Gunasekaran, 2011; Sogin & Gunderson, 1987). Likewise, the bacterial large 50S ribosomal subunit includes 23S rRNA, of approximately 2.9 kb, and the 120‐nucleotide 5S rRNA, while eukaryotic large subunit includes three different RNAs: the 25‐28S rRNA, at around 3.55–5.00 kb, the 5.8S rRNA of approximately 160 nucleotides and a 120‐nucleotide 5S rRNA (Biedka, Wu, LaPeruta, Gao, & Woolford Jr., 2017; Champney, 2001; Lee, Henry, & Yeh, 1983; Melnikov et al, 2012; Moore & Steitz, 2003).…”

Section: Introductionmentioning

confidence: 99%

Regulation of ribosomal protein genes: An ordered anarchy

et al. 2020

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Ribosomal protein genes are among the most highly expressed genes in most cell types. Their products are generally essential for ribosome synthesis, which is the cornerstone for cell growth and proliferation. Many cellular resources are dedicated to producing ribosomal proteins and thus this process needs to be regulated in ways that carefully balance the supply of nascent ribosomal proteins with the demand for new ribosomes. Ribosomal protein genes have classically been viewed as a uniform interconnected regulon regulated in eukaryotic cells by target of rapamycin and protein kinase A pathway in response to changes in growth conditions and/or cellular status. However, recent literature depicts a more complex picture in which the amount of ribosomal proteins produced varies between genes in response to two overlapping regulatory circuits. The first includes the classical general ribosome‐producing program and the second is a gene‐specific feature responsible for fine‐tuning the amount of ribosomal proteins produced from each individual ribosomal gene. Unlike the general pathway that is mainly controlled at the level of transcription and translation, this specific regulation of ribosomal protein genes is largely achieved through changes in pre‐mRNA splicing efficiency and mRNA stability. By combining general and specific regulation, the cell can coordinate ribosome production, while allowing functional specialization and diversity. Here we review the many ways ribosomal protein genes are regulated, with special focus on the emerging role of posttranscriptional regulatory events in fine‐tuning the expression of ribosomal protein genes and its role in controlling the potential variation in ribosome functions. This article is categorized under: Translation > Ribosome Biogenesis Translation > Ribosome Structure/Function Translation > Translation Regulation

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An RNA core in the 30S ribosomal subunit of and its structural and functional significance

Cited by 31 publications

References 45 publications

A ribonuclease-resistant region of 5S RNA and its relation to the RNA binding sites of proteins L18 and L25

A ribonuclease-resistant region of 5S RNA and its relation to the RNA binding sites of proteins L18 and L25

A ribonucleoprotein fragment of the 30 S ribosome ofE. colicontaining two contiguous domains of the 16 S RNA

Regulation of ribosomal protein genes: An ordered anarchy

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