SOLUBILIZATION AND HETEROGENEOUS NATURE OF PROTEINS FROM RIBOSOMES OF PEA-SEEDLING BUDS

1966 ◽  
Vol 44 (8) ◽  
pp. 1221-1233 ◽  
Author(s):  
A. M. MacQuillan ◽  
S. T. Bayley
Keyword(s):  
Amino Acid ◽  
Ribosomal Protein ◽  
Total Protein ◽  
Ribosomal Proteins ◽  
Subsequent Treatment ◽  
Electrophoretic Patterns ◽  
Heterogeneous Nature ◽  
Peptide Composition ◽  
Low Ionic Strength ◽  
Pea Seedling

The results of several procedures for solubilizing protein from pea-seedling ribosomes are described. Pancreatic ribonuclease (RNAase), alone at pH 8.0 and low ionic strength, solubilized 10%, whereas subsequent treatment with dilute HC1 solubilized a further 29%. RNAase in 8 M urea at pH 5.5 solubilized more than 90% of the ribosomal protein. After removal of ribonucleic acid fragments, all of this material, termed "total protein", remained in solution in 0.05 M acetate buffer at pH 5. Proteins solubilized by these three procedures were subjected to electrophoresis on starch–urea gels, amino acid analyses, and fingerprinting after digestion with trypsin and chymotrypsin. The protein soluble in RNAase probably contains only one or two components and is distinct in amino acid and peptide composition from the remainder of the ribosomal protein. Protein soluble in HC1 is representative of much of the "total protein" and both HC1-soluble and "total protein" are complex. Fingerprints showed that although RNAase-extracted protein and three fractions of "total protein" obtained by gel electrophoresis were different, they also possessed a number of peptides in common. It was concluded that the number of components in pea-ribosomal proteins is probably of the order of 16, the number of bands seen in gel-electrophoretic patterns.

Ribosomal proteins from goose reticulocytes are not histones

1968 ◽  
Vol 46 (12) ◽  
pp. 1507-1514 ◽  
Author(s):  
J. M. Neelin ◽  
G. Vidali
Keyword(s):  
Amino Acid ◽  
Ribosomal Protein ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ribosomal Proteins ◽  
Cross Contamination ◽  
Guanidinium Chloride ◽  
Electrophoretic Patterns ◽  
Starch Gel ◽  
Cell Fractions

Ribosomes were isolated from goose reticulocytes after lysis with saponin in 50 mM KCl, 1.5 mM MgCl2, 1 mM Tris, pH 7.5. Maximum yields of ribosomes were obtained about 4 days after injection of the birds with Phenylhydrazine, but ribosomal proteins did not vary with the stage of recovery.Ribosomal proteins (extracted with either HCl–urea or LiCl–urea) differed generally from histones (extracted with either HCl or HCl–urea) according to amino acid composition and to electrophoretic patterns in starch gel and in Polyacrylamide gel, but a few zones of ribosomal protein appeared to coincide electrophoretically with the main histone components. Since all of the former proteins were eluted unretarded from Amberlite CG-50 in 9% guanidinium chloride, in which all histones are adsorbed, we conclude that histones and ribosomal proteins are different classes of protein.The hazards of assuming chemical identities of proteins on the basis of limited electrophoretic evidence and the risks of misleading cross-contamination of cell fractions were demonstrated.

scholarly journals Halobacterium cutirubrum ribosomes. Properties of the ribosomal proteins and ribonucleic acid

1972 ◽  
Vol 130 (1) ◽  
pp. 103-110 ◽  
Author(s):  
L. P. Visentin ◽  
C. Chow ◽  
A. T. Matheson ◽  
M. Yaguchi ◽  
F. Rollin
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Soluble Fraction ◽  
Ribosomal Subunit ◽  
23S Rrna ◽  
Core Particle ◽  
Fractionation Procedure ◽  
Additional Protein ◽  
70S Ribosome ◽  
Low Ionic Strength

1. The 30S ribosomal subunit of the extreme halophile Halobacterium cutirubrum is unstable and loses 75% of its ribosomal protein when the 70S ribosome is dissociated into the two subunits. A stable 30S subunit is obtained if the dissociation of the 70S particle is carried out in the presence of the soluble fraction. 2. A fractionation procedure was developed for the selective removal of groups of proteins from the 30S and 50S subunits. When the ribosomes, which are stable in 4m-K+ and 0.1m-Mg2+, were extracted with low-ionic-strength buffer 75–80% of the 30S proteins and 60–65% of the 50S proteins as well as the 5S rRNA were released. The proteins in this fraction are the most acidic of the H. cutirubrum ribosomal proteins. Further extraction with Li+–EDTA releases additional protein, leaving a core particle containing either 16S rRNA or 23S rRNA and about 5% of the total ribosomal protein. The amino acid composition, mobility on polyacrylamide gels at pH4.5 and 8.7, and the molecular-weight distribution of the various protein fractions were determined. 3. The s values of the rRNA are 5S, 16S and 23S. The C+G contents of the 16S and 23S rRNA were 56.1 and 58.8% respectively and these are higher than C+G contents of the corresponding Escherichia coli rRNA (53.8 and 54.1%).

An intergenic G-rich region in Leishmania tarentolae kinetoplast maxicircle DNA is a pan-edited cryptogene encoding ribosomal protein S12

1992 ◽  
Vol 12 (1) ◽  
pp. 56-67
Author(s):  
D A Maslov ◽  
N R Sturm ◽  
B M Niner ◽  
E S Gruszynski ◽  
M Peris ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Sequence Similarity ◽  
Rich Region ◽  
Leishmania Tarentolae ◽  
Significant Sequence Similarity ◽  
The Family ◽  
Intergenic Regions ◽  
Ribosomal Protein S12

Six short G-rich intergenic regions in the maxicircle of Leishmania tarentolae are conserved in location and polarity in two other kinetoplastid species. We show here that G-rich region 6 (G6) represents a pan-edited cryptogene which contains at least two domains edited independently in a 3'-to-5' manner connected by short unedited regions. In the completely edited RNA, 117 uridines are added at 49 sites and 32 uridines are deleted at 13 sites, creating a translated 85-amino-acid polypeptide. Similar polypeptides are probably encoded by pan-edited G6 transcripts in two other species. The G6 polypeptide has significant sequence similarity to the family of S12 ribosomal proteins. A minicircle-encoded gRNA overlaps 12 editing sites in G6 mRNA, and chimeric gRNA/mRNA molecules were shown to exist, in agreement with the transesterification model for editing.

scholarly journals An intergenic G-rich region in Leishmania tarentolae kinetoplast maxicircle DNA is a pan-edited cryptogene encoding ribosomal protein S12.

1992 ◽  
Vol 12 (1) ◽  
pp. 56-67 ◽  
Author(s):  
D A Maslov ◽  
N R Sturm ◽  
B M Niner ◽  
E S Gruszynski ◽  
M Peris ◽  
...  
Keyword(s):  
Amino Acid ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Sequence Similarity ◽  
Rich Region ◽  
Leishmania Tarentolae ◽  
Significant Sequence Similarity ◽  
The Family ◽  
Intergenic Regions ◽  
Ribosomal Protein S12

Six short G-rich intergenic regions in the maxicircle of Leishmania tarentolae are conserved in location and polarity in two other kinetoplastid species. We show here that G-rich region 6 (G6) represents a pan-edited cryptogene which contains at least two domains edited independently in a 3'-to-5' manner connected by short unedited regions. In the completely edited RNA, 117 uridines are added at 49 sites and 32 uridines are deleted at 13 sites, creating a translated 85-amino-acid polypeptide. Similar polypeptides are probably encoded by pan-edited G6 transcripts in two other species. The G6 polypeptide has significant sequence similarity to the family of S12 ribosomal proteins. A minicircle-encoded gRNA overlaps 12 editing sites in G6 mRNA, and chimeric gRNA/mRNA molecules were shown to exist, in agreement with the transesterification model for editing.

Ribosomal RNA: the message or matrix for ribosomal proteins

1976 ◽  
Vol 54 (2) ◽  
pp. 192-193
Author(s):  
D. R. Miller ◽  
A. T. Matheson ◽  
L. P. Visentin
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Ribosomal Protein ◽  
Ribosomal Rna ◽  
Ribosomal Proteins ◽  
Protein Sequences ◽  
Amino Acid Sequences ◽  
16S Ribosomal Rna ◽  
Degree Of Similarity

The known nucleotide sequence of Escherichia coli 16S ribosomal RNA has been converted to amino acid sequences in all possible ways, and compared to known ribosomal protein sequences. The degree of similarity is precisely what one would expect by chance alone, providing additional evidence that ribosomal proteins cannot be coded for by ribosomal RNA.

Deficiency of dietary EAA preferentially inhibits mRNA translation of ribosomal proteins in liver of meal-fed rats

2001 ◽  
Vol 281 (3) ◽  
pp. E430-E439 ◽  
Author(s):  
Tracy G. Anthony ◽  
Ali K. Reiter ◽  
Joshua C. Anthony ◽  
Scot R. Kimball ◽  
Leonard S. Jefferson
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Serum Insulin ◽  
Control Diet ◽  
Mrna Translation ◽  
Initiation Factor ◽  
Liver Protein ◽  
Deficient Diet

The goal of these studies was to investigate the mechanisms by which amino acid supply regulates global rates of protein synthesis as well as the translation of ribosomal protein (rp) mRNAs in liver. In the experiments conducted, male weanling rats were trained over a 2-wk period to consume their daily food intake within 3 h. On day 14, rats were fed the control diet or an isocaloric, isonitrogenous diet lacking glycine, tryptophan, leucine, or the branched-chain amino acids (BCAA) for 1 h. Feeding Trp-, Leu-, or BCAA-deficient diets resulted in significant reductions in serum insulin, hepatic protein synthesis, eukaryotic initiation factor 2B (eIF2B) activity, and phosphorylation of eIF4E-binding protein 1 (4E-BP1) and ribosomal protein S6 kinase (S6K1). Phosphorylation of eIF2α was inversely related to eIF2B activity under all conditions. Alterations in the hepatic synthesis of rp were assessed by changes in the distribution of rp (S4, S8, L26) mRNAs across sucrose density gradients and compared with non-rp (β-actin, albumin) mRNAs. In all dietary treatments, non-rp mRNAs were mostly polysome associated. Conversely, the proportion of rp mRNAs residing in polysomes was two- to fivefold less in rats fed diets lacking tryptophan, leucine, or BCAA compared with rats fed the control diet. Total hepatic abundance of all mRNAs examined did not differ among treatment groups. For all parameters examined, there were no differences between rats fed the glycine-deficient diet and rats fed the control diet. The data suggest that essential amino acid (EAA) deficiency inhibits global rates of liver protein synthesis via a block in translation initiation. Additionally, the translation of rp mRNAs is preferentially repressed in association with decreased S6K1 phosphorylation.

N-Terminal Modifikation and Amino-Acid Sequence of the Ribosomal Protein HmaS7 fromHaloarcula marismortuiand Homology Studies to other Ribosomal Proteins

1993 ◽  
Vol 374 (1-6) ◽  
pp. 305-312 ◽  
Author(s):  
Sven KLUSSMANN ◽  
Peter FRANKE ◽  
Ulrike BERGMANN ◽  
Susanne KOSTKA ◽  
Brigitte WITTMANN-LIEBOLD
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ribosomal Protein ◽  
Ribosomal Proteins

Amino acid sequence of the ribosomal protein HS23 from the halophilicHaloarcula marismortui and homology studies to other ribosomal proteins

1995 ◽  
Vol 14 (4) ◽  
pp. 189-195 ◽  
Author(s):  
Sabine Engemann ◽  
Elke Herfurth ◽  
Ulrike Briesemeister ◽  
Brigitte Wittmann-Liebold
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ribosomal Protein ◽  
Ribosomal Proteins
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