Detachment of ribosomal proteins by salt

Spitnik‐Elson, Pnina; Atsmon, A

doi:10.1016/0022-2836(69)90214-9

Cited by 65 publications

(11 citation statements)

References 22 publications

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“…This is in contrast to the behaviour of ribosomes from the extreme halophile, Halobacterium cutirubrum, which maintain 'normal' monosomes and subunits in very high KC1 concentrations but alter drastically in lower salt concentrations [3]. It is also in contrast to the behaviour ofEscherichia coli ribosomes whose sedimentation behaviour and protein content are changed by salt concentrations of 0.5 M or higher [12][13][14] and which we have found to aggregate in gradients containing 1.0 M NaC1. Although E. coli grew almost as well in a salts glucose casamino acids medium containing 0.5 M NaC1 as in the absence of this salt, analytical ultracentrifuge experiments suggested that, in TMK containing 0.5 M NaC1 ribosomes from these cells fell apart into a mixture of ill-defined particles.…”

Section: Discussioncontrasting

confidence: 88%

Salt response of ribosomes of a moderately halophilic bacterium

1975

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Section: Discussioncontrasting

confidence: 88%

Salt response of ribosomes of a moderately halophilic bacterium

1975

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“…Our studies allowed us to accurately determine the subunit composition of endogenous mSWI/SNF complexes, revealing several new subunits as well as interacting proteins lacking the dedicated, non-exchangeable features of a subunit. We find that mSWI/SNF complexes have approximately the same stability as the ribosome 22,88,89 using urea-based denaturation methods. Hence, the function of BCL7A/B/C, BCL11A/B, BRD9, and SS18, similar to established mSWI/SNF subunits, should be considered in the context of mSWI/SNF complex function.…”

Section: Discussionmentioning

confidence: 83%

“…Remarkably, BCL7A/B/C, BCL11A/B, and BRD9 were bound to the mSWI/SNF complex with stabilities greater than or equal to most established subunits including BAF47, BAF155 and BAF170 (Fig. 1c), reflecting associations comparable to those of ribosomal subunits 22,23 . In addition, reciprocal IP's using antibodies to novel complex members revealed known mSWI/SNF components (Fig.…”

Section: Resultsmentioning

confidence: 96%

Proteomic and bioinformatic analysis of mammalian SWI/SNF complexes identifies extensive roles in human malignancy

et al. 2013

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Subunits of mammalian SWI/SNF (mSWI/SNF, also called BAF) complexes have recently been implicated as tumor suppressors in a number of human malignancies. To understand the full extent of their involvement, we conducted a proteomic analysis of purified endogenous mSWI/SNF complexes. Our studies revealed several new dedicated, stable subunits not found in the yeast SWI/SNF complex including Bcl7a, b and c, Bcl11a and b, Brd9 and SS18. Incorporating these novel members, we determined the frequency of mSWI/SNF subunit mutations in recent exome- and whole-genome sequencing studies of primary human tumors. Surprisingly, mSWI/SNF subunits are mutated in 19.6% of all human tumors reported in 44 exome sequencing studies. Our analysis suggests that specific subunits protect against cancer in specific tissues. In addition, we find that mutations to more than one subunit, which we define as a type of compound heterozygosity, are prevalent in certain cancers. Our studies demonstrate that mSWI/SNF is the most frequently mutated chromatin-regulatory complex (CRC) in human cancer and that in contrast to other known tumor suppressors and oncogenes surveyed, mSWI/SNF is broadly mutated, similar to TP53. Thus, proper functioning of these polymorphic chromatin regulatory complexes may constitute a major mechanism of human tumor suppression.

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“…It is known that high salt concentrations will remove specific groups of proteins from prokaryote ribosomes (Meselson, Nomura, Brenner, Davern & Schlessinger, 1964;Spitnik-Elson & Atsmon, 1969) and this has been shown for rat liver ribosomes (Reboud, Hamilton & Petermann, 1969;Grummt & Bielka, 1970;Clegg & Arnstein, 1970). Craven, Voynow, Hardy & Kurland (1969) have shown that some prokaryote ribosomal proteins, called fractional proteins, do not occur on all ribosomes all the time, as they are present in less than one mol/ mol of RNA in a given preparation.…”

mentioning

confidence: 98%

The proteins of Xenopus ovary ribosomes

Ford¹

1971

Biochemical Journal

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1. The preparation of ribosomes and ribosomal subunits from Xenopus ovary is described. 2. The yield of once-washed ribosomes (buoyant density in caesium chloride 1.601g.cm(-3); 44% RNA, 56% protein by chemical methods) was 10.1mg/g wet wt. of tissue. 3. Buoyant density in caesium chloride and RNA/protein ratios by chemical methods have been determined for ribosome subunits produced by 1.0mm-EDTA or 0.5m-potassium chloride treatment and also for EDTA subunits extracted with 0.5m-, 1.0m- or 1.5m-potassium chloride, 4. Analysis of ribosomal protein on acrylamide gels at pH4.5 in 6m-urea reveals 24 and 26 bands from small and large EDTA subunits respectively. The actual numbers of proteins are greater than this, as many bands are obviously doublets. 5. Analysis of the proteins in the potassium chloride extract and particle fractions showed that some bands are completely and some partially extracted. Taking partial extraction as an indication of possible doublet bands it was found that there were 12 and 20 such bands in the small and large subunits respectively, making totals of 36 and 46 proteins. 6. From the measured protein contents and assuming weight-average molecular weights for the proteins of large and small subunits close to those observed for eukaryote ribosomal proteins it is possible to compute the total numbers of protein molecules per particle. It appears that too few protein bands have been identified on acrylamide gels to account for all the protein in the large subunit, but probably enough for the small subunit.

show abstract

Detachment of ribosomal proteins by salt

Cited by 65 publications

References 22 publications

Salt response of ribosomes of a moderately halophilic bacterium

Salt response of ribosomes of a moderately halophilic bacterium

Proteomic and bioinformatic analysis of mammalian SWI/SNF complexes identifies extensive roles in human malignancy

The proteins of Xenopus ovary ribosomes

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