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)

The messenger RNAs for the outer membrane proteins in E. coli are more stable than the bulk of the messenger RNA s (Hirashima et al., 1973). Polysomes, enriched in those containing stable mRNAs have been isolated following rifampicin treatment and have been shown to contain quantitatively the same complement of ribosomal protein as normal polysomes. There is one exception: ribosomal protein S1 is present in larger amounts in the polysomes containing stable messengers. However, there are grounds for believing this finding to be an artifact. It is concluded that the differences between outer membrane protein synthesis and bulk protein synthesis are not due to a difference in the ribosomes.
Mol Gen Genet 1975
PMID:Analysis of the ribosomes engaged in the synthesis of the outer membrane proteins of Escherichia coli. 110 14

The nomenclature proposed by Otaka et al. (1968) for the 30S ribosomal protein components of Escherichia coli as separated by carboxymethyl(CM)-cellulose column chromatography was adopted in several papers in which the genetic loci for many 30S ribosomal proteins on the E. coli chromosome were determined. In order to compare these data with those obtained in other laboratories, the 30S ribosomal proteins fractionated by CM-cellulose chromatography were correlated with thestandard nomenclature proposed by Wittmann et al. (1971).
Mol Gen Genet 1975 Sep 15
PMID:Correlation of 30S ribosomal proteins of Escherichia coli fractionated on carboxymethyl-cellulose column chromatography to the standard nomenclature. 110 48

Analysis of in vivo phosphorylation of mouse liver ribosomal proteins was performed by two-dimensional polyacrylamide gel electrophoresis following 32P-injection. Our method is special and differs from other eukaryotic systems reported in that all proteins separated on the first dimension gel are completely solubilized, moving quantitatively to the second dimension gel. Only ribosomes from polysomes were used, ensuring analysis of ribosomes actively engaged in protein synthesis. We resolved sixty-five distinct proteins from ribosomes from membrane bound or free polysomes. In both cases radioautography revealed similar labeled patterns with one highly phosphorylated ribosomal protein and five marginally labeled spots.
Mol Biol Rep 1975 Oct
PMID:Analysis by two-dimensional polyacrylamide gel electrophoresis of the in vivo phosphorylation of ribosomal proteins derived from free and membrane-bound polysomes. 119 10

A metabolic system composed of nucleic acid enzymes is proposed to have existed prior to the evolution of ribosomal protein synthesis. Vestiges of these nucleic acid enzymes persist in contemporary coenzymes. This proposal rationalizes the fact that many coenzymes are nucleotides or heterocyclic bases which could be derived from nucleotides.
J Mol Evol 1976 Mar 29
PMID:Coenzymes as fossils of an earlier metabolic state. 126 63

The PET122 protein is one of three Saccharomyces cerevisiae nuclear gene products required specifically to activate translation of the mitochondrially coded COX3 mRNA. We have previously observed that mutations which remove the carboxy-terminal region of PET122 block translation of the COX3 mRNA but can be suppressed by unlinked nuclear mutations in several genes, two of which have been shown to code for proteins of the small subunit of mitochondrial ribosomes. Here we describe and map two more new genes identified as allele-specific suppressors that compensate for carboxy-terminal truncation of PET122. One of these genes, MRP17, is essential for the expression of all mitochondrial genes and encodes a protein of M(r) 17343. The MRP17 protein is a component of the small ribosomal subunit in mitochondria, as demonstrated by the fact that a missense mutation, mrp17-1, predicted to cause a charge change indeed alters the charge of a mitochondrial ribosomal protein of the expected size. In addition, mrp17-1, in combination with some mutations affecting another mitochondrial ribosomal protein, caused a synthetic defective phenotype. These findings are consistent with a model in which PET122 functionally interacts with the ribosomal small subunit. The second new suppressor gene described here, PET127, encodes a protein too large (M(r) 95900) to be a ribosomal protein and appears to operate by a different mechanism. PET127 is not absolutely required for mitochondrial gene expression and allele-specific suppression of pet122 mutations results from the loss of PET127 function: a pet127 deletion exhibited the same recessive suppressor activity as the original suppressor mutation. These findings suggest the possibility that PET127 could be a novel component of the mitochondrial translation system with a role in promoting accuracy of translational initiation.
Mol Gen Genet 1992 Oct
PMID:Suppression of carboxy-terminal truncations of the yeast mitochondrial mRNA-specific translational activator PET122 by mutations in two new genes, MRP17 and PET127. 127 74

We have designed a set of nine plasmids containing the Bacillus pumilis cat gene with one of three Shine-Dalgarno (SD) sequences (weak, strong or stronger) and one of three initiation codons (AUG, GUG or UUG). These constructions have been used to determine the effect of ribosomal protein S1, SD and initiation codon sequences and Escherichia coli ribosomal protein S1 on translation in vitro by E. coli and B. subtilis ribosomes. Translation of these nine constructions was determined with three types of ribosomes: E. coli containing ribosomal protein S1, E. coli depleted of S1, and B. subtilis which is naturally free of S1. E. coli ribosomes were able to translate all nine transcripts with variable efficiencies. B. subtilis and S1-depleted E. coli ribosomes were similar to each other and differed from non-depleted E. coli ribosomes in that they required strong or stronger SD sequences and were unable to translate any of the weak transcripts. Addition of S1 from either E. coli or Micrococcus luteus, a Gram-positive bacterium, enabled S1-depleted E. coli ribosomes to translate mRNAs with weak SD sequences but had no effect on B. subtilis ribosomes. AUG was the preferred initiation codon for all ribosome types; however, B. subtilis ribosomes showed greater tolerance for the non-AUG codons than either type of E. coli ribosome. The presence of a strong or stronger SD sequence increased the efficiency by which E. coli ribosomes could utilize non-AUG codons.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Microbiol 1992 Nov
PMID:The effect of ribosomal protein S1 from Escherichia coli and Micrococcus luteus on protein synthesis in vitro by E. coli and Bacillus subtilis. 128 1

The intron-containing gene encoding human ribosomal protein S6 (rpS6), the major phosphoprotein in the mammalian ribosome, has been cloned. Using a PCR based cloning strategy we have isolated the rpS6 intron-containing gene in the presence of its many processed pseudogenes and determined the DNA sequence of the entire gene and its upstream and downstream flanking regions. The human rpS6 gene is 3979 bp in length and comprises six exons. Despite lacking a consensus TATA box, primer extension analysis indicates that the start of transcription is located at a single C residue within an 11 bp oligopyrimidine tract. The first exon, which contains the ATG start codon, is 48 bp in length. The DNA sequence in the 5' region of the gene has features of a CpG-rich island. Using fluorescence in situ hybridization (FISH) analysis the position of the rpS6 gene has been sublocalized to human chromosome 9p21. The similarities and differences between rpS6 and other previously characterized ribosomal protein genes are discussed.
Hum Mol Genet 1992 Nov
PMID:The organization of the intron-containing human S6 ribosomal protein (rpS6) gene and determination of its location at chromosome 9p21. 130 Nov 64

The long terminal repeat of Moloney murine leukemia virus (MuLV) contains the upstream conserved region (UCR). The UCR core sequence, CGCCATTTT, binds a ubiquitous nuclear factor and mediates negative regulation of MuLV promoter activity. We have isolated murine cDNA clones encoding a protein, referred to as UCRBP, that binds specifically to the UCR core sequence. Gel mobility shift assays demonstrate that the UCRBP fusion protein expressed in bacteria binds the UCR core with specificity identical to that of the UCR-binding factor in the nucleus of murine and human cells. Analysis of full-length UCRBP cDNA reveals that it has a putative zinc finger domain composed of four C2H2 zinc fingers of the GLI subgroup and an N-terminal region containing alternating charges, including a stretch of 12 histidine residues. The 2.4-kb UCRBP message is expressed in all cell lines examined (teratocarcinoma, B- and T-cell, macrophage, fibroblast, and myocyte), consistent with the ubiquitous expression of the UCR-binding factor. Transient transfection of an expressible UCRBP cDNA into fibroblasts results in down-regulation of MuLV promoter activity, in agreement with previous functional analysis of the UCR. Recently three groups have independently isolated human and mouse UCRBP. These studies show that UCRBP binds to various target motifs that are distinct from the UCR motif: the adeno-associated virus P5 promoter and elements in the immunoglobulin light- and heavy-chain genes, as well as elements in ribosomal protein genes. These results indicate that UCRBP has unusually diverse DNA-binding specificity and as such is likely to regulate expression of many different genes.
Mol Cell Biol 1992 Jan
PMID:Cloning of a negative transcription factor that binds to the upstream conserved region of Moloney murine leukemia virus. 130 93

The gene encoding Aedes albopictus ribosomal protein L8 was isolated using a cDNA probe. Based on the deduced amino acid sequence, rpL8 has a mass of 28,605 Da, a pI of 11.97, and contains 9.6% Arg and 11.9% Lys. The rpL8 gene spans 1229 nucleotides, and contains three exons measuring 73, 150, and 648 nucleotides. The first intron is 293 nucleotides long and interrupts an 85-nucleotide untranslated leader sequence. The AUG codon is located 12 nucleotides downstream of the 5'-end of the second exon. Separating the second and third exon is a 65-nucleotide intron. The major transcription initiation site, identified by primer extension and polymerase stop reactions, mapped 378 nucleotides upstream from the AUG start codon; minor initiation sites were also detected. The DNA sequence upstream of the rpL8 gene was T-rich, but conventional TATA and CAAT boxes were absent. This is the first molecular analysis of a mosquito ribosomal protein gene.
Insect Mol Biol 1992
PMID:Sequence analysis of a mosquito ribosomal protein rpL8 gene and its upstream regulatory region. 134 79

Mammalian liver development is accompanied by a transition from rapid growth in the fetus to a quiescent state in the adult. However, extensive proliferation can be induced in the adult liver by partial hepatectomy. In this study, we examined the regulation of ribosomal protein (rp) gene expression in the developing and regenerating rat liver. Our results indicate that the translation of rp mRNAs is selectively repressed by about 70% upon development from fetal to adult life, as illustrated by the decrease in ribosomal loading. In addition, the relative abundance of these mRNAs, like that of several other, but not all, housekeeping mRNAs, declines during development through a posttranscriptional mechanism. When liver cells commence growth following partial hepatectomy, translation of rp mRNAs is resumed to near-maximal capacity, as judged by their very efficient recruitment into polysomes. The concomitant increase in the abundance rp mRNAs under these circumstances is achieved by a posttranscriptional mechanism. The apparent fluctuations in the translation efficiency of rp mRNAs are accompanied by parallel changes in the expression of the genes encoding the initiation factors eIF-4E and eIF-4A. Our results indicate that selective translational control of rp mRNAs in mammals is not confined to manipulated cells in culture but constitutes an important regulatory mechanism operating in vivo in the course of liver development and regeneration.
Mol Cell Biol 1992 May
PMID:Selective translational control and nonspecific posttranscriptional regulation of ribosomal protein gene expression during development and regeneration of rat liver. 137 10


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