scholarly journals SYNTHESIS OF A COLCHICINE-BINDING PROTEIN DURING THE HELA CELL LIFE CYCLE

1969 ◽  
Vol 43 (2) ◽  
pp. 371-373 ◽  
Author(s):  
Elliott Robbins ◽  
Michael Shelanski
Keyword(s):  
Life Cycle ◽  
Hela Cell ◽  
Binding Protein ◽  
Cell Life

scholarly journals ABSENCE OF TRANSLATIONAL CONTROL OF HISTONE SYNTHESIS DURING THE HELA CELL LIFE CYCLE

1970 ◽  
Vol 45 (3) ◽  
pp. 509-513 ◽  
Author(s):  
Thoru Pederson ◽  
Elliott Robbins
Keyword(s):  
Life Cycle ◽  
Hela Cell ◽  
Cytosine Arabinoside ◽  
Translational Control ◽  
Messenger Rna ◽  
Deoxyribonucleic Acid ◽  
S Phase ◽  
Cell Life ◽  
Histone Synthesis ◽  
G1 Cells

The cell-free synthesis of histone-like polypeptides has been achieved using a selected class of small polyribosomes as the only particulate fraction. This synthesis is prevented if the deoxyribonucleic acid (DNA) inhibitor, cytosine arabinoside, is added to the cells prior to disruption, and it is not detected when the cytoplasm used is derived from postmitotic (G1) cells. When the 100,000 g supernate from pure metaphase populations was compared with that from S phase cells, the cell-free synthesis of histone-like polypeptides in the presence of S phase polyribosomes remained unchanged. These data suggest that, except for the histone messenger RNA-ribosome complex, the cytoplasmic factors requisite for histone synthesis are present throughout the cycle, and that the shut-off of this synthesis is not under translational control.

Poliovirus Replication during HeLa Cell Life Cycle

1972 ◽  
Vol 237 (73) ◽  
pp. 114-116 ◽  
Author(s):  
T. EREMENKO ◽  
A. BENEDETTO ◽  
P. VOLPE
Keyword(s):  
Life Cycle ◽  
Hela Cell ◽  
Cell Life

scholarly journals Borrelia burgdorferi Lacking BBK32, a Fibronectin-Binding Protein, Retains Full Pathogenicity

2006 ◽  
Vol 74 (6) ◽  
pp. 3305-3313 ◽  
Author(s):  
Xin Li ◽  
Xianzhong Liu ◽  
Deborah S. Beck ◽  
Fred S. Kantor ◽  
Erol Fikrig
Keyword(s):  
Life Cycle ◽  
Borrelia Burgdorferi ◽  
Deletion Mutant ◽  
Binding Protein ◽  
Kanamycin Resistance ◽  
Binding Activity ◽  
Mammalian Host ◽  
Wild Type ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

ABSTRACT BBK32, a fibronectin-binding protein of Borrelia burgdorferi, is one of many surface lipoproteins that are differentially expressed by the Lyme disease spirochete at various stages of its life cycle. The level of BBK32 expression in B. burgdorferi is highest during infection of the mammalian host and lowest in flat ticks. This temporal expression profile, along with its fibronectin-binding activity, strongly suggests that BBK32 may play an important role in Lyme pathogenesis in the host. To test this hypothesis, we constructed an isogenic BBK32 deletion mutant from wild-type B. burgdorferi B31 by replacing the BBK32 gene with a kanamycin resistance cassette through homologous recombination. We examined both the wild-type strain and the BBK32 deletion mutant extensively in the experimental mouse-tick model of the Borrelia life cycle. Our data indicated that B. burgdorferi lacking BBK32 retained full pathogenicity in mice, regardless of whether mice were infected artificially by syringe inoculation or naturally by tick bite. The loss of BBK32 expression in the mutant had no adverse effect on spirochete acquisition (mouse-to-tick) and transmission (tick-to-mouse) processes. These results suggest that additional B. burgdorferi proteins can complement the function of BBK32, fibronectin binding or otherwise, during the natural spirochete life cycle.

Characterization and purification of lupus antigen La, and RNA-binding protein

1985 ◽  
Vol 5 (3) ◽  
pp. 586-590
Author(s):  
A M Francoeur ◽  
E K Chan ◽  
J I Garrels ◽  
M B Mathews
Keyword(s):  
Hela Cell ◽  
Gel Electrophoresis ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
In Vitro Translation ◽  
Cell Protein ◽  
Two Dimensional Gel Electrophoresis ◽  
La Antigen

HeLa cell La antigen, an RNA-binding protein, was characterized by using two-dimensional gel electrophoresis. Eight isoelectric forms (pI 6 to 7) were observed, many containing phosphate. An in vitro translation product similar in size and antigenicity was identified. The HeLa cell protein purified by using an assay based on ribonucleoprotein reconstitution with adenovirus VA RNAI also comprised several isoelectric forms.

A cell-specific factor represses stimulation of transcription in vitro by transcriptional enhancer factor 1

1994 ◽  
Vol 14 (8) ◽  
pp. 5290-5299
Author(s):  
S Chaudhary ◽  
C Brou ◽  
M E Valentin ◽  
N Burton ◽  
L Tora ◽  
...  
Keyword(s):  
Hela Cell ◽  
Binding Protein ◽  
Activation Function ◽  
Tata Binding Protein ◽  
Lymphoid Cells ◽  
Specific Factor ◽  
Transcriptional Enhancer ◽  
Cell Extracts ◽  
A Cell

Transcription in HeLa cell extracts in vitro was stimulated 8- to 10-fold by a recombinant chimera, GAL-TEF-1, consisting of the DNA-binding domain of GAL4 and the activation function of the HeLa cell activator TEF-1. In contrast, only a 2- to 3-fold stimulation was obtained with GAL-TEF-1 in extracts from BJA-B lymphoid cells. Stimulation by GAL-TEF-1 in BJA-B extracts was dramatically increased by the addition of immunopurified HeLa cell TFIID, suggesting that BJA-B TFIID lacks or contains lower quantities of a TATA-binding-protein-associated factor(s) required for the activity of the TEF-1 activation function. However, chromatography, immunopurification, and transcriptional reconstitution experiments indicated that BJA-B extracts did not lack the previously identified TATA-binding-protein-associated factors required for TEF-1 activity but rather contained a negatively acting factor(s) which inhibited transactivation by GAL-TEF-1. These results indicate that the relative lack of activity of the TEF-1 activation function in vitro in BJA-B cell extracts does not result from the absence of positively acting factors from the presence of a cell-specific negatively acting factor(s).

scholarly journals Glassy dynamics in models of confluent tissue with mitosis and apoptosis

Soft Matter ◽  
2019 ◽  
Vol 15 (44) ◽  
pp. 9133-9149 ◽  
Author(s):  
Michael Czajkowski ◽  
Daniel M. Sussman ◽  
M. Cristina Marchetti ◽  
M. Lisa Manning
Keyword(s):  
Cell Death ◽  
Life Cycle ◽  
Cell Division ◽  
Epithelial Tissue ◽  
Vertex Model ◽  
Glassy Dynamics ◽  
Cell Life ◽  
Active Vertex

Using a new Active Vertex Model of confluent epithelial tissue, we investigate the effect of cell division and cell death on previously identified glassy dynamics and establish how fast the cell life cycle must be in order to disrupt the observed dynamical signatures of glass-like behavior.

scholarly journals NUCLEOLAR AND NUCLEAR RNA SYNTHESIS DURING THE CELL LIFE CYCLE IN MONKEY AND PIG KIDNEY CELLS IN VITRO

1967 ◽  
Vol 33 (2) ◽  
pp. 273-279 ◽  
Author(s):  
Jane L. Showacre ◽  
W. G. Cooper ◽  
D. M. Prescott
Keyword(s):  
Life Cycle ◽  
Rna Synthesis ◽  
Kidney Cells ◽  
Pig Kidney ◽  
Rna Labeling ◽  
Cell Life ◽  
Nuclear Rna ◽  
Nucleolar Rna ◽  
Pig Kidney Cells

The incorporation of 5-3H-uridine and 5-3H-cytidine into nucleolar and nonnucleolar RNA in the nucleus of monkey and pig kidney cells was measured in vitro during the cell life cycle. Time-lapse cinematographic records were made of cells during asynchronous exponential proliferation, in order to identify the temporal position of individual cells in relation to the preceding mitosis. Immediately following cinematography, cells were labeled with uridine-3H and cytidine-3H for a short period, fixed, and analyzed by radioautography. Since the data permit correlation of the rate of RNA labeling with the position of a cell within the cycle, curves could be constructed describing the rate of RNA synthesis over the average cell cycle. RNA synthesis was absent in early telophase, and rose very abruptly in rate in late telophase and in very early G1 in both the nucleus and the reconstituting nucleolus. Thereafter, through the G1 and S periods the rate of nuclear RNA synthesis rose gradually. When we used a 10-min pulse, there was no detectable change in the rate for nucleolar RNA labeling in monkey kidney cells during G1 or S. When we used a 30-min labeling time, the rate of nucleolar RNA labeling rose gradually in pig kidney cells. With increasing time after mitosis, the data became more variable, which may, in part, be related to the variation in generation times for individual cells.

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