Changes in the rate of RNA synthesis during the cell cycle

Salem, Cherine; El‐Alfy, Mohamed; Leblond, C. P.

doi:10.1002/(sici)1097-0185(199801)250:1<6::aid-ar2>3.0.co;2-4

Cited by 13 publications

(7 citation statements)

References 22 publications

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“…The amount of rRNA in the cells exhibiting mitotic figures (Me 1 and Me 2 in Figures 3a, 3c, and 3e) markedly decreased. These results coincided with the changes in the rate of RNA synthesis during the cell cycle described in detail by Salem et al (1998). For examining the proliferative activity of cells, the use of histone mRNA is recommended because it degrades rapidly after S-phase is completed (Slowinski et al 2002).…”

Section: Rrna As a Positive Control For Ishsupporting

confidence: 56%

Quantification of In Situ Hybridization Signals in Rat Testes

Kimura

Kosaka

Nomura

et al. 2004

J Histochem Cytochem.

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S U M M A R YWe performed basic research into quantifying in situ hybridization (ISH) signals in rat testis, a suitable organ for the quantification because germ cells undergo synchronized development and show stage-specific gene expression. In this model experiment, rRNA was selected as the hybridizable RNA in paraffin sections. Specimens fixed with Bouin's fixative and hybridized with digoxygenin-labeled probes could easily be analyzed quantitatively through "posterization" of the images. The amount of rRNA hybridized with the probe was greatest in early primary spermatocytes, followed by pachytene primary spermatocytes, then diplotene spermatocytes, and finally by secondary spermatocytes and spermatids. The amounts reached low levels in metaphase, anaphase, and telophase of meiotic division and early step 1 spermatids, and then slightly increased during spermiogenesis. ISH rRNA staining was a useful parameter for evaluation of the quantitative analysis of mRNA and the levels of hybridizable RNA in tissue sections.

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Section: Rrna As a Positive Control For Ishsupporting

confidence: 56%

Quantification of In Situ Hybridization Signals in Rat Testes

Kimura

Kosaka

Nomura

et al. 2004

J Histochem Cytochem.

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“…Thereafter, in early G 1 , PUM2 might reassociate with the P2P‐R mRNA to again repress its translation. Future studies will have to evaluate this possibility, and future studies also will have to determine if high levels of P2P‐R influences transcription and translation control mechanisms that are known to be modified in mitotic cells (Salem et al, 1998; Sciortino et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

P2P‐R expression is genetically coregulated with components of the translation machinery and with PUM2, a translational repressor that associates with the P2P‐R mRNA

Scott

White-Grindley

Ruley

et al. 2004

Journal Cellular Physiology

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P2P-R is a nuclear protein with potential functional roles in the control of gene expression and mitosis. The P2P-R protein also interacts with the p53 and Rb1 tumor suppressor proteins. To search for additional functional associations of P2P-R, we employed the WebQTL database that contains the results of cDNA microarray analysis on forebrain, cerebellum, and hematopoietic stem cell (HSC) specimens of multiple BXD recombinant inbred strains of mice. Using WebQTL, gene products were identified that show genetically based coexpression with P2P-R. Initial studies identified general groups of mRNAs that share common functional roles and high covariation in expression with P2P-R. These functional groups involved the regulation of transcription, nucleotide binding, translation control, and ion transport. The findings related to translational mechanisms were further evaluated. In HSCs, expression of P2P-R mRNA demonstrates an impressive expression correlation with a group of gene products associated with translation; high expression of P2P-R specifically was associated with decreased expression of 29 ribosomal protein mRNAs. In all three tissues that were screened using the WebQTL database, a strong positive expression covariance between P2P-R and the Pum2 gene product also was observed. PUM2 is a member of the highly conserved Puf family of RNA binding proteins that often function as gene-specific translation regulators. The ability of Puf proteins to repress translation is mediated by their binding to specific elements located in the 3' untranslated region (UTR) of their target mRNAs. To assess the functional significance of the strong genetic correlation in expression of P2P-R and PUM2, the 3' UTR of the P2P-R mRNA was analyzed and found to contain one perfect consensus and two near-perfect consensus PUM2 binding sequences. PUM2 pull-down methods combined with reverse transcription and RT-PCR confirmed that PUM2 does indeed bind P2P-R mRNA. These results suggest that P2P-R expression may be translationally regulated by PUM2 and that P2P-R may modulate translation by influencing ribosomal protein gene expression. This study represents the first description of a RNA target for mammalian Puf proteins and the first molecular confirmation of information obtained using the WebQTL database.

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“…The second discovery of the current research is that immunoreactive P2P‐R protein can be detected at > 10‐fold higher levels in mitotic cells than in G 0 cells using Western blotting techniques but that P2P‐R mRNA expression is not correspondingly increased. Confocal microscopy also showed that in mitotic cells, P2P‐R is localized to the periphery of chromosomes in mitotic cells that do not contain nucleoli and show markedly repressed RNA metabolism (Salem et al, 1998). Preliminary data using cells expressing transfected green fluorescent protein‐tagged P2P‐R also show the localization of P2P‐R at the periphery of mitotic chromosomes.…”

Section: Discussionmentioning

confidence: 99%

P2P‐R protein localizes to the nucleolus of interphase cells and the periphery of chromosomes in mitotic cells which show maximum P2P‐R immunoreactivity

Gao

Witte

Scott

2002

Journal Cellular Physiology

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P2P-R is a nuclear protein that can bind both p53 and Rb1. Its functions include roles in the control of RNA metabolism, apoptosis, and p53-dependent transcription. The expression of P2P-R also is repressed in G1 arrested terminally differentiated cells. The current studies therefore evaluated if P2P-R undergoes cell cycle-associated changes in its abundance and/or localization. Western blots show that relative to G0 quiescent cells, P2P-R protein levels are higher in populations of G2/M cells prepared by the physiological parasynchronization technique of serum deprivation followed by serum stimulation. More striking is the > 10-fold enrichment of P2P-R protein in specimens of highly purified mitotic cells prepared by the mitotic shake-select technique, or by synchrony with the mitotic spindle disruption agents nocodazole or vinblastine. These changes in P2P-R protein occur without a concomitant change in P2P-R mRNA expression suggesting that P2P-R immunoreactivity increases during mitosis. Confocal microscopy next established the localization of P2P-R to nucleoli in interphase cells and at the periphery of chromosomes in mitotic cells that lack nucleoli. The high levels of P2P-R localized to the periphery of chromosomes in mitotic cells suggest that P2P-R shares characteristics with other nucleolar proteins that associate with the periphery of chromosomes during mitosis. These include: nucleolin, B23, Ki67, and fibrillarin.

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Changes in the rate of RNA synthesis during the cell cycle

Abstract: Cells synthesize RNA during the interphase, but at a variable rate with a peak in S. The synthesis proceeds in a majority of the cells at prophase, but only in a few of them at prometaphase and metaphase, and in none at anaphase and telophase.

Cited by 13 publications

References 22 publications

Quantification of In Situ Hybridization Signals in Rat Testes

Quantification of In Situ Hybridization Signals in Rat Testes

P2P‐R expression is genetically coregulated with components of the translation machinery and with PUM2, a translational repressor that associates with the P2P‐R mRNA

P2P‐R protein localizes to the nucleolus of interphase cells and the periphery of chromosomes in mitotic cells which show maximum P2P‐R immunoreactivity

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