Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Polyacrylamide gel electrophoresis of the 30S ribosomal proteins derived from six streptomycin resistant strains indicates that each mutation alters the same ribosomal protein (str-r protein). Preliminary data utilizing SDS gels indicates that the str-r protein has a molecular weight between 10,000 and 20,000 daltons. No significant differences could be detected between the molecular weight of the str-r protein when it is derived either from a sensitive or from a resistant strain, including those derived from strains carrying multisite mutations of different genetic size. We have estimated the size of the multisite str-r mutations to be less than 30 base pairs. Two factor crosses with str-r markers in the trans position demonstrate recombination frequencies expected of closely linked, intragenic markers although cotransfer frequencies, of these same markers from the cis position, are very low. It is concluded that the cotransfer frequencies represent a marker effect and possible explanations are discussed. A reinterpretation of the genetic map of the pneumococcal str-r locus is presented.
Mol Gen Genet 1977 May 20
PMID:A comparison of the genetic and physical size of the streptomycin resistance locus in Pneumococcus. 1 58

The conditionally lethal mutation, 2861 mis, has been mapped inside the ribosomal protein gene cluster at 72 minutes on the Escherichia coli chromosome and was found to cotransduce at 97% with rpsE (S5). The 2861 mis mutation leads to thermosensitivity and impaired assembly in vivo of 30S ribosomal particles at 42 degrees C. The strain carrying the mutation has an altered S 17 ribosomal protein; the mutational alteration involves a replacement of serine by phenylalanine in protein S 17. Spontaneous reversion to temperature independence can restore the normal assembly in vivo of 30 S ribosomal subunits at 42 degrees C and the normal chromatographical behaviour of the S 17 ribosomal protein in vitro. We conclude therefore that the 2861 mis mutation affects the structural gene for protein S 17 (rpsQ).
Mol Gen Genet 1979 Mar 09
PMID:A missense mutation in the gene coding for ribosomal protein S17 (rpsQ) leading to ribosomal assembly defectivity in Escherichia coli. 10 17

We have isolated, after ethylmethanesulfonate mutagenesis, several chromosomal mutations causing resistance to tetracycline in Bacillus subtilis. These mutations fall into two classics, tetA and tetB. 30 S ribosomal protein S10 shows an altered mobility on two-dimensional acrylamide gels in cells bearing the former type of mutation. Ribosomes from these cells show elevated levels of resistance to tetracycline in vitro as measured by polyuridine dependent polyphenylalanine synthesis. The tetA locus maps adjacent to the tuf gene in the B. subtilis ribosomal protein gene cluster. Cells with the tetB mutation do not show any altered ribosomal protein, and their ribosomes are as sensitive, in vitro, to tetracycline as ribosomes isolated from wild type cells. The tetB mutation has been mapped proximal to cysA14.
Mol Gen Genet 1979
PMID:Chromosomal mutations causing resistance to tetracycline in Bacillus subtilis. 11 96

In a merodiploid strain of Escherichia coli heterozygous for the ribosomal protein genes spc and str, deletions were observed preventing the expression of either gene but permitting the expression of the other. This suggests that the spc and str genes are in separate transcriptional units.
Mol Gen Genet 1976 Mar 22
PMID:Deletions of ribosomal protein genes in Escherichia coli merodiploids heterozygous for resistance to streptomycin and spectinomycin. 13 8

Alterations in the ribosomes of sucrose-dependent spectinomycin-resistant (Sucd-Spcr) mutants of Escherichia coli were studied. Subunit exchange experiments showed that 30S subunits were responsible for the resistance of ribosomes to spectinomycin in all Sucd-Spcr mutants tested. Proteins of 30S ribosomes were analyzed by carboxymethyl cellulose column chromatography based on their elution positions. Mutants YM22 and YM93 had an altered 30S ribosomal protein component, S5, and mutant YM50 had an altered protein, S4. Although a shift of elution position was not detected for all the 30S ribosomal proteins from mutant YM101, the amount of protein S3 was appreciably lowered in the isolated 30S subunits. A partial reconstitution experiment with protein S3 prepared from both the wild-type strain and YM101 revealed that the mutant had altered protein S3 which is responsible for the spectinomycin resistance. These alterations in 30S subunits are discussed in relation to the interaction between ribosomes and the cytoplasmic membrane.
Mol Gen Genet 1977 Sep 21
PMID:Interaction of the cytoplasmic membrane and ribosomes in Escherichia coli; altered ribosomal proteins in sucrose-dependent spectinomycin-resistant mutants. 14 65

Recent results with Neurospora crassa show that one protein (S-5, mol wt 52,000) associated with the mitochondrial (mit) small ribosomal subunit is translated within the mitochondria (Lambowitz et al. 1976. J. Mol. Biol. 107:223-253). In the present work, Neurospora mit ribosomal proteins were analyzed by two-dimensional gel electrophoresis using a modification of the gel system of Mets and Bogorad. The results show that S-5 is present in near stoichiometric concentrations in high salt (0.5 MKCl)-washed mit small subunits from wild-type strains. S-5 is among the most basic mit ribosomal proteins (pI greater than 10) and has a high affinity for RNA under the conditions of the urea-containing gel buffers. The role of S-5 in mit ribosome assembly was investigated by an indirect method, making use of chloramphenicol to specifically inhibit mit protein synthesis. Chloramphenicol was found to rapidly inhibit the assembly of mit small subunits leading to the formation of CAP-30S particles which sediment slightly behind mature small subunits (LaPolla and Lambowitz. 1977. J. Mol. 116: 189-205). Two-dimensional gel analysis shows that the more slowly sedimentaing CAP-30S particles are deficient in S-5 and in several other proteins, whereas these proteins are present in normal concentrations in mature small subunits from the same cells. Because S-5 is the only mit ribosomal protein whose synthesis is directly inhibited by chloramphenicol, the results tentatively suggest that S-5 plays a role in the assembly of mit small subunits. In addition, the results are consistent with the idea that S-5 stabilizes the binding of several other mit small subunit proteins. Two-dimensional gel electrophoresis was used to examine mit ribosomal proteins from [poky] and six additional extra-nuclear mutants with defects in the assembly of mit small subunits. The electrophoretic mobility of S-5 is not detectably altered in any of the mutants. However, [poky] mit small subunits are deficient in S-5 and also contain several other proteins in abnormally low or high concentrations. These and other results are consistent with a defect in a mit ribosomal constituent in [poky].
 ...
PMID:Mitochondrial ribosome assembly in Neurospora. Two-dimensional gel electrophoretic analysis of mitochondrial ribosomal proteins. 15 27

The nucleic acid binding and unwinding properties of wild-type Escherichia coli ribosomal protein S1 have been compared to those of a mutant form and a large trypsin-resistant fragment, both reported recently [J. Mol. Biol. 127, 41-45 (1979) and J. Biol. Chem. 254, 4309-4312 (1979). The mutant (m1-S1) contains 77% and the fragment (S1-F1) 66% of the polypeptide chain length (approximately 600 amino acid residues) of protein S1. The mutant is active in protein synthesis in vitro; the fragment, although retaining one or more of the functional domains of S1, is inactive in protein synthesis. We find that m1-S1 is is almost as effective as S1 in binding to poly(rU), phage MS2 RNA and simian virus 40 (SV40) DNA, and in unfolding poly(rU) and the helical structures present in MS2 RNA and phi X174 viral DNA. S1-F1, however, binds to poly(rU) and denatured SV40 DNA, but not to MS2 RNA. It unfolds neither poly(rU), nor the residual secondary structure of MS2 RNA or phi X174 viral DNA. Thus, there appears to be a correlation between the loss in ability of S1 to unwind RNA and the loss in its ability to function in protein synthesis.
 ...
PMID:Nucleic acid binding and unfolding properties of ribosomal protein S1 and the derivatives S1-F1 and m1-S1. 23 41

The transcriptional activity of the DNA sequences coding for certain ribosomal proteins has been measured in Escherichia coli. Two partial diploid strains were isolated from mating of a recA, argD, aroE recipient and an Hfr with an origin at 69.5 min. One contained an F' element carrying the genes from 69.5 to 72.7 min including the rpsL locus (72.4) and the second was diploid for the genes from 69.5 to 71.5 min but did not include any mapped ribosomal protein loci. The molecular weights of the plasmids were estimated to be 140 and 110 x 10(6) daltons, respectively. The extent of in vivo transcription of the chromosomal genes on the plasmid and the ribosomal protein mRNA fraction of the total cellular RNA weer calculated from DNA-RNA liquid hybridization experiments using both DNA and RNA excess procedures. The results indicated a high degree of transcriptional activity concentrated in the ribosomal protein sequences with 83% of the F' chromosomal sequences transcribed into mRNA products representing about 0.12% of the total cellular RNA.
Mol Gen Genet 1977 Jan 18
PMID:Transcription of ribosomal protein genes carried on F' plasmids of Escherichia coli. 32 Apr 54

26 cold-resistant revertants of a cold-sensitive Escherichia coli mutant with an altered ribosomal protein S8 were analyzed for their ribosomal protein pattern by two-dimensional polyacrylamide gel electrophoresis. It was found that 16 of them had acquired the apparent wild-type form of protein S8, one exhibits a more strongly altered SC than the original mutant and two revertants regained the wildtype form of S8 and, in addition, possess alterations in protein L30. The ribosomes of the residual revertants showed no detectable difference from those of the parental S8 mutant. The mutation leading to the more strongly altered S8 was genetically not separable from the primary S8 mutation; this indicates that both mutations are very close to each other or at the same site. The structural gene for ribosomal protein L30 was mapped relative to two other ribosomal protein genes (for proteins S5 and S8) by the aid of one of the L30 mutants: The relative order obtained is: aroE....rpmD(L30)....rpsE(S5)....rpsH(S8)....rpsL(S12). The L30 mutation impairs growth and ribosomal assembly at 20 degrees C and is therefore the first example of a mutant with defined 50S alteration that has (partial) cold-sensitive ribosome assembly. A double mutant was constructed which possesses both the S8 and the L30 mutations. It was found that the L30 mutation had a slight antagonistic effect on the growth inhibition caused by the S8 mutation. Thus the L30 mutants might have possibly arisen from the original S8 mutant first as S8/L30 double mutants which was followed by the loss of the original S8 lesion.
Mol Gen Genet 1977 Apr 29
PMID:Cold-sensitive growth of a mutant of Escherichia coli with an altered ribosomal protein S8: analysis of revertants. 32 86

Using an in vitro preparation for protein synthesis, we have studied the effect of the ribosomal protein S1 from Escherichia coli on the synthesis of the coat protein of the RNA-containing phages Qbeta and MS2, on that of an "early" and a "late" enzyme encoded by the DNA containing phage T7, and on that of anthranilate synthetase, an enzyme encoded by the bacterial tryptophan operon. Our results indicate that for the synthesis of these five proteins the presence of S1 is required. From these results we conclude that S1 is an essential protein for the translation of bacterial and bacteriophage messenger RNA.
Mol Gen Genet 1977 May 20
PMID:The effect of the ribosomal protein S1 from Escherichia coli on the synthesis in vitro of bacterial-, DNA phage- and RNA phage proteins. 32 5


1 2 3 4 5 6 7 8 9 10 Next >>