The isolation and characterization of a macromolecular ribonucleoprotein from yeast

Chao, Fu-Chuan; Schachman, H. K.

doi:10.1016/0003-9861(56)90334-4

Cited by 203 publications

(47 citation statements)

References 15 publications

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“…The sedimentation coefficient at infinite dilution was found to be 80 x 10-13 see. (Chao & Schachman, 1956); a similar value was also reported by Bowen, Dagley, Sykes & Wild (1961). In solutions poor in Mg and Cay the 80 S ribosome dissociated into 60 and 40 S particles (Chao, 1957); papain action led to a similar breakdown (Morgan, Greenspan & Cunningham, 1963 …”

Section: Introductionsupporting

confidence: 61%

Sedimentation Coefficients of Yeast Ribosomes

Ley

1964

Journal of General Microbiology

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SUNZMARYThe corrected sedimentation coefficients, expressed as (S20, a)O, of ribosomes from nine different yeasts, representing a wide taxonomic range, were found to be 51.5 f 2.4, 68.6 f 3.3 and 86.7 & 2.9 x see. Very small quantities of a faster (approximately 128 x sec.) and a slower particle were sometimes detected. Yeast ribosomes have thus sedimentation coefficients which are distinctly different from bacterial ribosomes.

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Section: Introductionsupporting

confidence: 61%

Sedimentation Coefficients of Yeast Ribosomes

Ley

1964

Journal of General Microbiology

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“…Their sedimentation coefficient is 85 S (7) as compared to 80 S for yeast (15), pea seedling (16), and liver ribosomes (17), and to 70 S for bacterial RNP particles (18)(19)(20)(21). Moreover, there is no evidence that they are comprised, like other ribosomes, of 30 to 40 S and 50 to 60 S subunits (17-21) which dissociate at low, and copolymerize at high, Mg ++ concentrations.…”

Section: Discussionmentioning

confidence: 99%

Cytochemical Study on the Pancreas of the Guinea Pig

Siekevitz

Palade

1962

The Journal of Cell Biology

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Pancreatic ribosomes (guinea pig) aggregate and lose upon treatment with polyamincs, particularly spcrmine, their bound secretory enzymcs. Spcrmine, at 0.5 mM, for example, causes the releasc of about 85 per cent of the chymotrypsinogcn and RNasc, and from 85 to 100 pcr cent of the ribosomal amylase. At the same time, the particles lose about 10 per cent of their RNA, 7 to 24 per cent of thcir total protein, and from 75 to 100 per cent of their Mg ++. Obscrvations with the electron microscope confirm the heavy agglutinating of the ribosomes but otherwise show little change in the structure of the particles. Using radioactive spcrminc it was found that, concomitant with thc loss of bound cnzymcs and Mg ++ from the ribosomes, spermine became bound to the particle. The extent of binding ranged from 0.29 to 1.49 #moles per I0/zmoles RNA-P. The bound radioactivc spcrmine can bc rcmovcd by subsequent treatment of the ribosomes with GTP, ATP, or P-P, which treatment also removes most of the RNA of the particles, leaving behind ribosomes with a much lower RNA/protein ratio. From this evidence it was inferred that spcrminc, in releasing the Mg ++ of the particle, bccomes salt-linked to the free phosphate hydroxyl groups of the RNA. Frcshly isolatcd pancreatic and hcpatic ribosomes contain very littlc spcrminc, about 0.1 to 0.2 pmolcs polyaminc/10/zmoles RNA-P. The results are discussed in terms of the linkages between the structural protein, the bound sccretory enzymes, and the RNA of the ribosomes.

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“…3C and reference 15). Ribosomes, especially rRNAs, extensively interact with Mg 2ϩ ions that neutralize the negative charges of rRNA backbone (17), and starvation of Mg 2ϩ ions has a negative impact on the integrity and assembly of ribosomes (7,8,21). This may explain why starvation of Mg 2ϩ in the absence of either RrmJ or Der in E. coli causes disintegration of 50S subunits.…”

Section: Emerging Evidence Indicates That Many Escherichia Colimentioning

confidence: 99%

Interaction of an Essential Escherichia coli GTPase, Der, with the 50S Ribosome via the KH-Like Domain

Hwang

Inouye

2010

J Bacteriol

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Der, an essential Escherichia coli tandem GTPase, has been implicated in 50S subunit biogenesis. The rrmJ gene encodes a methyltransferase that modifies the U2552 residue of 23S rRNA, and its deletion causes a severe growth defect. Peculiarly, overexpression of Der suppresses growth impairment. In this study, using an rrmJ-deletion strain, we demonstrated that two GTPase domains of Der regulate its association with 50S subunit via the KH-like domain. We also identified a region of Der that is critical for its specific interaction with 50S subunit. Emerging evidence indicates that many Escherichia coliGTPases play critical roles in ribosome biogenesis (6). For example, E. coli Era consists of a conventional GTP-binding domain and a KH domain (an RNA-binding domain) with a consensus VIGXXGXXI sequence (9). The direct interaction between Era and 16S rRNA was demonstrated by structural studies of a Thermus thermophilus 30S ribosomal subunit complexed with Era (24). Peculiarly, Era was shown to suppress the cold-sensitive cell growth of the rbfA-deletion strain whose gene product resembles a KH domain and plays an important role in 30S subunit assembly at low temperature (13, 16). A unique GTPase subfamily of Der (double Era-like GTPase; also known as EngA) is conserved only in eubacteria. We have previously demonstrated that Der is cofractionated with 50S subunits in a GTP-dependent manner and that Der plays a critical role in 50S subunit maturation at a later biogenesis step (15).Interestingly, both GTP-binding domains (G domains) were essential for cell growth; moreover, the two G domains function cooperatively, suggesting that GTP-induced conformational changes and GTPase activity are essential for cell viability as well as function (1, 15). The X-ray crystal structures of two Der orthologs from Thermotoga maritima and Bacillus subtilis revealed that the C-terminal domain has a topology similar to that of a KH domain without a consensus sequence motif and is flanked by two G domains (22, 23). It was suggested that the GTP-bound form of YphC (a Der ortholog in B. subtilis) triggers a dramatic conformational change, which favors an interaction with negatively charged ribonucleic acids by exposing a positively charged KH-like domain with a high pI value (14, 22).Overexpression of E. coli Der functionally suppressed the slow growth defect of a deletion strain of the rrmJ gene, whose gene product is a methyltransferase, modifying the U2552 residue in the A loop of 23S rRNA in an intact 50S subunit (5, 26). Even though ⌬rrmJ (strain HB23) is viable, it causes a serious defect of cell growth by accumulating 50S and 30S ribosomal subunits at the expense of 70S ribosomes. Thus, overexpression of Der seems to overcome its weak interaction with 50S subunits that are unmethylated at U2552. In this study, using an ⌬rrmJ strain as a genetic background, we tried to elucidate the nature of the functional regulation of two G domains and the KH-like domain. We further characterized the KH-like domain by random mutagenesis and iden...

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The isolation and characterization of a macromolecular ribonucleoprotein from yeast

Cited by 203 publications

References 15 publications

Sedimentation Coefficients of Yeast Ribosomes

Sedimentation Coefficients of Yeast Ribosomes

Cytochemical Study on the Pancreas of the Guinea Pig

Interaction of an Essential Escherichia coli GTPase, Der, with the 50S Ribosome via the KH-Like Domain

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