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  • 1
    Electronic Resource
    Electronic Resource
    Correlation between 30S ribosomal proteins of Bacillus stearothermophilus and Escherichia coli (1973)
    Springer
    Molecular genetics and genomics 127 (1973), S. 191-195 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The 30S ribosomal proteins from Bacillus stearothermophilus strains 799 and 10 were purified and correlated with those from E. coli by comparing their two-dimensional electrophoretic mobility, immunological cross-reaction, molecular weight, amino acid composition and partial amino acid sequence. A high degree of similarity was observed among the proteins from these taxonomically distant bacterial species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00333666
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  • 2
    Electronic Resource
    Electronic Resource
    Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsl) and L13 (rplM) of Escherichia coil (1985)
    Springer
    Molecular genetics and genomics 200 (1985), S. 350-350 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425448
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  • 3
    Electronic Resource
    Electronic Resource
    Further temperature-sensitive mutants ofEscherichia coli with altered ribosomal proteins (1977)
    Springer
    Molecular genetics and genomics 152 (1977), S. 239-243 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Various alterations in ribosomal proteins were detected in forty-one mutants ofE. coli isolated as temperature-sensitive mutants. Out of these, six are new classes of mutants harboring mutations in proteins S3, L5, L7 (L12), L29, L30 and L33. One of them apparently lacks protein L7 of the large subunit. These mutants together with those reported previously (Isono et al., 1976) total one hundred and one ribosomal mutants in thirty different proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00693076
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of the generimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 inEscherichia coli K12 (1989)
    Springer
    Molecular genetics and genomics 217 (1989), S. 281-288 
    Details
    ISSN: 1617-4623
    Keywords: Escherichia coli ; Ribosomal protein S6 ; Addition of glutamic acid residues ; Cloning and sequencing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ribosomal protein S6 of wild-type strains ofEscherichia coli contains up to six glutamic acid residues at its C-terminus. The first two residues are encoded by the structural gene for this protein (rpsF) and the rest are added post-translationally. Mutants deficient in this modification were isolated and characterized genetically and biochemically. The S6 protein in these mutants appeared to contain only two glutamic acid residues at the C-terminus as expected. The mutated gene was termedrimK and was mapped at 18.7 min betweencmlA andaroA. TherimK gene was cloned into a cosmid vector and its nucleotide sequence determined. Analysis of the transcriptional and translational products of this gene indicates that it encodes a protein with an Mr of 31.5 kDa and that it forms an operon with a gene encoding a 24 kDa protein. AnrpsF mutant containing a Glu to Lys replacement in the second residue from the C-terminus of protein S6 was isolated. The S6 protein of this mutant was apparently inaccessible to the RimK modification system. This indicates that the RimK modification system requires the wild-type amino acid sequence at least in the C-terminal region of ribosomal protein S6.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02464894
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  • 5
    Electronic Resource
    Electronic Resource
    Ribosomal protein modification in Escherichia coli (1980)
    Springer
    Molecular genetics and genomics 177 (1980), S. 645-651 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A mutant of Escherichia coli K12 has been isolated which shows an alteration in the ribosomal protein S18. Genetic analyses have revealed that the mutation causing this alteration maps at 99.3 min of the E. coli genetic map, between dnaC and deo. This indicated that the mutation has occurred in a gene different from the structural gene for this protein which has been located at 94 min. From the N-terminal amino acid sequence analysis it is concluded that the mutation has resulted in loss of the N-terminal acetyl group of this protein. The gene which is affected in this mutant is termed rimI that most likely specifies an enzyme acetylating the N-terminal alanine of protein S18. The mutation does not affect the acetylation of two other ribosomal proteins, S5 and L12, both of which are known to be acetylated in wild-type E. coli K12.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00272675
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  • 6
    Electronic Resource
    Electronic Resource
    Cloning and nucleotide sequencing of the genes for ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli (1985)
    Springer
    Molecular genetics and genomics 198 (1985), S. 279-282 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The genes for the ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli have been cloned into a λ phage vector termed L47.1. The two genes were identified by infecting UV-light irradiated cells with the resultant phages and analyzing the protein products by two-dimensional gel electrophoresis. Suitable DNA fragments of the isolate were cloned subsequently into M13 phage vectors and their nucleotide sequence was determined by the dideoxy method. It is evident that the two genes form a transcriptional unit, the rplM gene being promoter-proximal. There is a typical signal sequence for transcriptional termination after the rpsI gene. The codon usage pattern in the two genes is similar to other ribosomal protein genes of E. coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00383007
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  • 7
    Electronic Resource
    Electronic Resource
    Cloning, characterization, and physical location of the rplY gene which encodes ribosomal protein L25 in Escherichia coli K12 (1991)
    Springer
    Molecular genetics and genomics 226 (1991), S. 341-344 
    Details
    ISSN: 1617-4623
    Keywords: Escherichia coli ; Ribosomal protein ; Nucleotide sequence ; Physical map
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The rplY gene of Escherichia coli K12 encoding ribosomal protein L25 was cloned from the ordered clone bank and located at coordinate 2,291 kb on the physical map of E. coli. Determination of the nucleotide sequence indicated that the coding region contains 285 nucleotide pairs including a translational initiator and terminator. The amino acid sequence of the protein deduced from the nucleotide sequence matched completely the sequence determined for ribosomal protein L25. The coding region was found to be preceded by a typical promoter-like sequence and was followed by a DNA region capable of forming a secondary structure characteristic of a transcriptional terminator. Thus, the gene was concluded to constitute a transcriptional unit (operon). A preliminary analysis by Northern blot supported this conclusion. The codnn usage pattern of the rplY gene is characteristic of the ribosomal protein genes in E. coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00273625
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  • 8
    Electronic Resource
    Electronic Resource
    Mutations affecting the structural genes and the genes coding for modifying enzymes for ribosomal proteins in Escherichia coli (1978)
    Springer
    Molecular genetics and genomics 165 (1978), S. 15-20 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Temperature-sensitive mutants of an Escherichia coli K-12 strain PA3092 have been isolated following mutagenesis with nitrosoguanidine, and their ribosomal proteins analyzed by two-dimensional gel electrophoresis This method was found to be very efficient in obtaining mutants with various structural alterations in ribosomal proteins. Thus a total of some 160 mutants with alterations in 41 different ribosomal proteins have so far been isolated. By characterizing these mutants, we could isolate, not only those mutants with alterations in the structural genes for various ribosomal proteins, but also those with impairments in the modification of proteins S5, S18 and L12. Furthermore, a mutant has been obtained which apparently lacks the protein S20 (L26) with a concomitant reduction to a great extent of the polypeptide synthetic activity of the small subunit. The usefulness of these mutants in establishing the genetic architecture of the genes coding for the ribosomal proteins and their modifiers is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00270371
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  • 9
    Electronic Resource
    Electronic Resource
    Ribosomal protein modification in Escherichia coli (1981)
    Springer
    Molecular genetics and genomics 183 (1981), S. 473-477 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Among mutants of E. coli selected for temperaturesensitive growth, four were found to possess alterations in ribosomal proteins L7/L12. Of these, three apparently lack protein L7, the acetylated form of protein L12. Genetic analyses have revealed that the mutation responsible for this alteration maps at a locus around 34 min of the current E. coli genetic map, which is clearly different from the location for the structural gene for protein L7/L12 which is situated at 89 min. Hence, the gene affected in these mutants was termed rimL. Tryptic and thermolysin fingerprints of the protein L12 purified from the rimL mutants showed a profile indistinguishable from that of wild-type protein. It was found that the acetylase activity specific for protein L12 was negligible, when assayed in vitro, in the high-speed supernatant prepared from mutant cells. These results indicated that the three mutants contain mutations in the gene rimL that codes for an acetylating enzyme specific for ribosomal protein L12.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268767
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  • 10
    Electronic Resource
    Electronic Resource
    Unstable mutations caused by regional tandem multiplications in the gene for ribosomal protein S4 show thermosensitivity in Escherichia coli (1985)
    Springer
    Molecular genetics and genomics 199 (1985), S. 265-270 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequence of the gene rpsD for the ribosomal protein S4 of three thermosensitive mutants of Escherichia coli K 12 was determined. It was found that two of them contained regional multiplications of a nucleotide sequence within the gene rpsD. In one case, it is a duplication of a 31 nucleotide stretch and in another it is a triplication of a 41 nucleotide stretch. The thermosensitive phenotype of the two mutants is unstable and reverts at the frequency of approximately 10-4. The revertants regain the wild-type nucleotide sequence. We postulate that the two mutant genes that contain regional multiplications possibly take an intra-strands secondary structure, which is cleaved to regenerate the wild-type sequence, probably during DNA replication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330268
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