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At least 433 records · Page 24Linked to original sources
PubMed2000

Cell cycle regulation and RNA polymerase II.

The cell cycle and transcription by RNA polymerase II (RNAP II) are closely related. They utilize shared components. RNAP II transcriptional activity is modulated during the cell cycle. Cell cycle dependent changes in the phosphorylation status of the carboxyl-terminal domain (CTD) of the largest subunit of RNAP II (RNAP II-LS) alter transcription. Several CTD kinases are members of the cyclin-dependent kinase (cdk) superfamily, including p34cdc2 (cdk1), cdk7, cdk8, and cdk9. Each of these cdks, with their respective cyclin partners, have been linked to cell cycle regulatory events. Other CTD kinases such as casein kinase II (CKII) and c-abl have also been implicated in cell cycle dependent modifications of the CTD. In addition, the stalling of RNAP II complexes at DNA lesions helps stimulate p53 accumulation which largely determines the cell's DNA damage response, including cell cycle arrest. Alzheimer's disease pathology results partially from activation of mitotic cdks in postmitotic neurons which can phosphorylate RNAP II-LS and other targets.

Animals↗
PubMed1999

Identification and characterization of a novel protein that regulates RNA-protein interaction.

In a previous study [Nachaliel et al., 1993], we identified an RNA-binding protein (RBP) in FTO-2B rat hepatoma cells whose activity was stimulated upon the dissociation of a protein factor. We report in this article that the RBP is a complex protein of about 400 kDa, composed of RNA-binding subunit(s) (RBS), and regulatory subunit(s) (RS). We purified the RS to near-homogeneity (Mr approximately 25,000) and determined the amino acid sequence of a peptide derived from RS. On the basis of this sequence information, the cDNA for RS was obtained. Recombinant RS protein expressed in Escherichia coli had the capacity to bind RBS and inhibit its RNA-binding activity. The cDNA contains the complete coding sequence because the recombinant protein has the same electrophoretic mobility as that of the native RS in SDS-polyacrylamide gels. Sequence comparison showed that RS is almost identical to DJ-1, a recently discovered protein with an oncogenic potential, and CAP1, a rat sperm protein. However, the protein does not contain any known motifs that can provide a clue as to its exact function. Indirect immunofluorescence analyses showed that in addition to the cytoplasm, where RS is associated with microtubular filaments, the polypeptide is localized to the cell nucleus. The possible role of RS is discussed.

Amino Acid Sequence↗
PubMed1975

Regulation of RNA synthesis in Escherichia coli. III. Degradation of guanosine 5'-diphosphate 3'-diphosphate in cold-shocked cells.

Cold-shocked cells of Escherichia coli can degrade intracellularly accumulated guanosine 5'-diphosphate 3'-diphosphate (ppGpp). The rate of ppGpp degradation is governed, as in whole cells, by the spoT gene; a rapid breakdown reaction is associated with the presence of the spoT+ allele and at least a five-fold slower decay occurs in spoT-minus mutants. The two degradation reactions in shocked cells display the following similarities: (i) the rates of degradation are equivalent to whole cell estimates, (ii) both require a full complement of activated amino acids, (iii) both are dependent upon supplements in the reaction mixture which stimulate the availability of energy-rich compounds and (iv) neither is inhibited by concentrations of ribosomal antibiotics which severely restrict protein synthesis. Apart from characteristic rate differences, decay of ppGpp in shocked cells derived from spoT-minus strains is discerned from spoT+ mediated decay in shocked cells by sensitivity to high concentrations of tetracycline and by manganese ion dependence.

Alleles↗
PubMed2004

[Selective effect of inductors of apoptosis on the endoribonuclease activity of 26S proteasomes and alpha-RNP particles in K562 cells: possible involvement of 26S proteasomes and alpha-RNP in the regulation of RNA stability].

It has been shown that endoribonuclease activity of alpha-RNP particles and 26S proteasomes are changed under the action of inductors of programmed cell death. Treatment of K562 cells with inductors of apoptosis--doxorubicin (adriamycin) and diethylmaleate--lead to a significant stimulation of RNAse activity of alpha-RNP and to reduction of proteasome RNase activity. The enzymatic activity under study has been shown to be specifically and selectively dependent on phosphorylation of subunits of alpha-RNP particles and 26S proteasomes. The characteristics of RNAse activity of different subpopulations of proteasomes differ. The specificity of a subpopulation of proteasomes exported from the cell has been demonstrated. Proteasome and alpha-RNP involvement in the coordinated control of stability of various specific messenger RNA molecules is suggested, and one of the mechanisms of this control might be the export of specific subpopulation of proteasomes from the cell.

Apoptosis↗
PubMedDate not supplied

[Regulation of RNA synthesis in the rat heart in L-thyroxine toxicosis and hypothyroidism; the role of RNA-polymerases and the template activity of chromatin].

It is shown that L-thyroxin applied to rats has induced in them development of pronounced cardiac hypertrophy accompanied by an increase in the total amount of nucleic acids in the myocardium (per organ) and enhancement of the RNA synthesis rate. It is confirmed by a considerable rise of the intensity of the labelled uridine incorporation into RNA without alteration of the specific radioactivity in a pool of free nucleotides and by the growth of the RNA-polymerase I activity. When L-thyroxin toxicosis lasts for four weeks and heart weight has not already increased the content of nucleic acids remains high, the rate of the label incorporation into RNA lowering down to the normal level. The activity of RNA-polymerase I is almost twice as low as that under thyrotoxicosis lasting for a week. In this case the matrix activity of chromatin tested by exogenous RNA-polymerase III of the rat gets lower. Under mercasolyl-induced hypothyrosis the heart weight decreases as well as the amount of nucleic acids, RNA synthesis intensity (by 40%) and RNA-polymerase I activity in it. The data obtained testify to the versatile effect of the thyroid hormones on RNA biosynthesis in the cardiac muscle and on the activity of both the RNA-polymerases and chromatin matrix.

Animals↗
PubMed1978

[Regulation of RNA replication in RNA-containing bacteriphages. RNA synthesis in coat protein polar mutants].

The synthesis of RNA by polar coat protein mutants f2sus3 and Qbetaam12 under suppressor (Escherichia coli S26R1E, Su+-1; H12R8a Su+-3) and non-suppressor (E. coli AB259; S26) conditions was examined. It was demonstrated that the synthesis of viral RNA under non-suppressor conditions in the presence of rifamycin produced the same gaussian pattern of rates as the synthesis of RNA by wild type phage or non-polar coat protein mutants. However, the total amount of RNA was decreased approximately 10-fold and the peak of RNA synthesis was displaced 7--10 min later. The number of infective centers was reduced also 10-fold indicating that a certain time-lapse was required to overcome the polarity of the parental RNA, this process being of single occurrence, exclusively on the parental RNA, but not on the progeny strains. As a consequence, it was concluded that the initiation of translation at the replicase cistron starts on the nascent RNA chains within the replicative complexes and not on the fully-synthesized templates with their complete secondary structure. The data obtained are not in contradiction with the hypothesis concerning the role of the repressor complex II (replicase-RNA) to slow down the synthesis of replicase and RNA in the coat protein mutants. The polarity can not be responsible probably for the blocking of the replicase cistron on the nascent chain following the block of coat protein cistron. Therefore, it appears appropriate to assume the existence of two binding sites for the replicase as repressor which is in keeping with the conclusions of Weissmann and co-workers.

Coliphages↗