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  • 1
    Electronic Resource
    Electronic Resource
    Isolation and characterization of twenty-three ribosomal proteins from large subunits of yeast (1979)
    s.l. : American Chemical Society
    Biochemistry 18 (1979), S. 5787-5793 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00593a007
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  • 2
    Electronic Resource
    Electronic Resource
    Primary structures of ribosomal protein YS25 from Saccharomyces cerevisiae and its counterparts from Schizosaccharomyces pombe and rat liver (1985)
    s.l. : American Chemical Society
    Biochemistry 24 (1985), S. 7418-7423 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00346a058
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  • 3
    Electronic Resource
    Electronic Resource
    Examination of protein sequence homologies: I. ElevenEscherichia coli L7/L12-type ribosomal “A” protein sequences from eubacteria and chloroplast (1985)
    Springer
    Journal of molecular evolution 21 (1985), S. 339-345 
    Details
    ISSN: 1432-1432
    Keywords: Prokaryotes ; Ribosomal proteins ; Correlation coefficient ; Sequence homology ; Protein evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Seven complete and four partial sequences ofEscherichia coli L7/L12-type ribosomal “A” proteins obtained from various bacteria (E. coli, Bacillus subtilis, Micrococcus lysodeikticus, Rhodopseudomonas spheroides, Desulfovibrio vulgaris, Streptomyces griseus, Bacillus stearothermophilus, Clostridium pasteurianum, Arthrobacter glacialis, andVibrio costicola) and spinach chloroplast have been reexamined using a computer program that searches for homologous tertiary structures. Comparison matrices for the sequences show that they match the sequence ofE. coli L7 (EL7) if one assumes the insertion or deletion of certain residues at sites corresponding to residues 1, 38, 49, and 92 of EL7. That two additional insertion points are found only in the spinach chloroplast protein suggests that the chloroplast protein probably diverged from the bacterial forms. Further phylogenetic relationships among these 11 prokaryote-type “A” proteins are discussed with respect to average correlation coefficients computed, taking into account the existence of the gaps.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02115652
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  • 4
    Electronic Resource
    Electronic Resource
    Examination of protein sequence homologies: II. SixEscherichia coli L7/L12-type ribosomal “A” protein sequnces from eukaryotes and metabacteria, contrasted with those from prokaryotes (1985)
    Springer
    Journal of molecular evolution 22 (1985), S. 342-350 
    Details
    ISSN: 1432-1432
    Keywords: Eukaryotes ; Prokaryotes ; Ribosomal proteins ; Correlation coefficient ; Protein evolution ; Transposition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Four complete and three partial sequences ofE. coli L7/L12-type ribosomal “A” proteins obtained from four eukaryotes (Saccharomyces cerevisiae, Artemia salina, rat liver, and wheat germ), two metabacteria (Halobacterium cutirubrum andMethanobacterium thermoautotrophicum), and the prokaryoteEscherichia coli have been compared using a computer program that searches for homologous tertiary structures. Comparison matrices show that eukaryotic sequences sequentially match each other if deletions and/or insertions of certain residues (gaps) are assumed at specific sites corresponding to residues 36, 51, 72, and 94 ofS. cerevisiae protein YL44c. This is similar to what was previously found in prokaryotes. Metabacteria, which exhibit eukaryote-type sequences, must have separated from the eukaryotes in ancient times, because an additional deletion site is found in their sequences and their sequences have low correlation coefficients with those of all the other eukaryotes. When the eukaryote-type A proteins (110–111 residues) are compared withE. coli L7/L12 (120 residues) four groups of well-matching segments are found. It was deduced that the eukaryote-type A proteins had regenerated from the prokaryote types by a transposition and several deletions, resulting in the eukaryote-type lengths. The correspondence between the eukaryotic and prokaryotic proteins, as well as that among eukaryotic proteins themselves, is discussed in terms of protein evolution. In addition, ribosomal protein YL35 fromS. cerevisiae has been compared with RL37 from rat liver, with results indicating five well-matching parts separated by four gaps, one of which consists of 20 residues. These results contrasts with those previously reported by Lin et al. No prokaryotic counterparts to these ribosomal proteins have yet been identified.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02115690
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  • 5
    Electronic Resource
    Electronic Resource
    Examination of protein sequence homologies: III. Ribosomal protein YS25 fromSaccharomyces cerevisiae and its counterparts fromSchizosaccharomyces pombe, rat liver, andEscherichia coli (1986)
    Springer
    Journal of molecular evolution 23 (1986), S. 337-342 
    Details
    ISSN: 1432-1432
    Keywords: Eukaryotes ; Prokaryotes ; Correlation coefficient ; Transpositions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The sequences of the ribosomal proteins YS25, SP-S28, RL-S21, and Ec-S6, fromSaccharomyces cerevisiae, Schizosaccharomyces pombe, rat liver, andEscherichia coli, respectively, have been examined using a computer program that searches for homologous tertiary structures. Matrices of comparisons among the eukaryotic sequences show that they match each other sequentially without any internal gaps. The average values of the correlation coefficients obtained from the comparison matrices are higher for the first halves of the sequences than for the latter halves. This result suggests that the first halves of the sequences may represent a more important domain than the latter halves. The comparison matrices between the eukaryotic and bacterial sequences of ribosomal proteins, however, do not show sequentially arranged homology, though there are six well-matching segments arranged in different orders in the two types of sequences. This implies that the eukaryotic sequences of the ribosomal protein were reconstituted by two internal transpositions and six deletions of 4–12 residues each from the ancestral sequence during the divergence between bacterial and eukaryotic genes. These findings may give insight into structural and quantitative studies of evolutionary divergence between eukaryotes and prokaryotes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02100643
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  • 6
    Electronic Resource
    Electronic Resource
    Alteration of ribosomal protein S5 from two spectinomycin-resistant mutants of Bacillus subtilis: Deletion of one amino acid residue (1982)
    Springer
    Molecular genetics and genomics 185 (1982), S. 205-206 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ribosomal protein S5 was isolated from Bacillus subtilis ATCC 6633 (wild-type) and two spectinomycin-resistant mutants (BSPC 31 and BSPC 61). Analyses of the protein revealed that in each of these mutants one of the two consecutive arginine residues (position 29 or 30 in the wild-type) is missing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330787
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  • 7
    Electronic Resource
    Electronic Resource
    Yeast ribosomal proteins (1984)
    Springer
    Molecular genetics and genomics 195 (1984), S. 544-546 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Two proteins, YL41 and YL43, were isolated from 80S ribosomes of Saccharomyces cerevisiae by filtration through a Sephacryl S-200 column and by chromatography on a column of carboxymethylcellulose. Their amino acid compositions are presented. Twenty-four proteins including these two proteins were subjected to sequence analyses by automated Edman degradation. Amino-terminal amino acid sequences were determined for 17 proteins, YS3, YS9, YS23, YS24, YS29, YL6, YL8, YL11, YL15, YL17, YL23, YL28, YL33, YL37, YL39, YL41, and YL43. YL41, which has a 72.7% lysine and arginine content, was found to be particular to eukaryotic ribosomes. The aminotermini of another seven proteins, YS2, YS5, YS8, YS12, YS13, YS20, and YS27, were suggested to be blocked. Comparison of the amino-terminal sequences with all other ribosomal protein sequences so far available indicates that YS9 shows sequence homology to rat liver ribosomal protein S8 (Wittmann-Liebold et al. 1979).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00341461
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  • 8
    Electronic Resource
    Electronic Resource
    Yeast ribosomal proteins: VII. Cytoplasmic ribosomal proteins from Schizosaccharomyces pombe (1983)
    Springer
    Molecular genetics and genomics 191 (1983), S. 519-524 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The cytoplasmic ribosomal proteins from a fission yeast Schizosaccharomyces pombe were analysed by two-dimensional polyacrylamide gel electrophoresis. Seventy-three protein species were identified in the 80S ribosome, and named SP-S1 to SP-S33 and SP-L1 to SP-L40 in the small and large subunits, respectively. Many of these proteins could be correlated to those of Saccharomyces cerevisiae on the basis of their electrophoretic mobilities. Eleven proteins were isolated from the 80S ribosome, and their amino acid compositions were determined. Of these, SP-S6, SP-L1, SP-L12, SP-L15, SP-L17, SP-L27, SP-L36 and SP-L40c and d were sequenced from their amino-termini. SP-S28 and SP-L2 appear to have their amino-termini blocked. These results were compared with the data available for the S. cerevisiae and rat liver ribosomal proteins. The S. cerevisiae counterparts of the eight proteins mentioned above were found to be YS4, YL1, YL10, YL14, YL35, YL40 and YL44c and d, respectively. The rat liver counter-parts of SP-S6, SP-L1, SP-L27 and SP-L40c and d were the rat S6, L4, L37 and P2, respectively. Comparison of the partial sequences of these ribosomal proteins suggests that these two yeasts are relatively far apart, phylogenetically.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425772
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  • 9
    Electronic Resource
    Electronic Resource
    Peptide analyses of a protein component, 50-8, of 50s ribosomal subunit from erythromycin resistant mutants of Escherichia coli and Escherichia freundii (1972)
    Springer
    Molecular genetics and genomics 114 (1972), S. 14-22 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Chromatographic analyses on a Dowex 50x8 column of tryptic digests of the mutationally altered 50-8 protein component from several erythromycin resistant (ery r) mutants of Escherichia coli and Escherichia freundii have been performed. It was found that (1) the difference in the elution profile of the altered components detected with carboxymethyl cellulose column chromatography reflects the difference in their amino acid sequence, (2) the structural change(s) of the 50-8 protein from three E. coli ery r mutants examined seems to exist only in the same single peptide fragment and (3) the primary structure of the 50-8(R) protein of E. freundii (ery s: wild type) differs from that of E. coli Q13 (ery s) and the structural change in 50-8(R) component of E. freundii caused by the ery r mutation was found to take place in different peptide fragments from that in which the mutational change of the E. coli 50-8 component occurred.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268742
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  • 10
    Electronic Resource
    Electronic Resource
    Ribosomes from spiramycin resistant mutants of Escherichia coli Q13 (1972)
    Springer
    Molecular genetics and genomics 114 (1972), S. 23-30 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutants from Escherichia coli Q13 were selected for resistance to leucomycin, tylosin or spiramycin. Most of the mutants so selected exhibited cross resistance to all the macrolide antibiotics tested including erythromycin. A few mutants however seem to be less resistant to erythromycin. One mutant, QSP008, was highly resistant to tylosin, leucomycin and spiramycin but relatively sensitive to erythromycin. Another mutant, QSP006, was highly resistant to spiramycin but less resistant to erythromycin, tylosin and leucomycin. This selective resistance of cells to specific antibiotics could be due to the extent of conformational alteration of their ribosomes, which may be demonstrated by the extent of 14C-erythromycin binding to these ribosomes. The ribosomes from QSP008 cells were found to contain an altered 50-8 protein of the 50s ribosomal subunit, while in the ribosomes from QSP006 no such protein change could be detected by the methods used.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268743
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