Chicken histone H5 inhibits transcription and replication when introduced into proliferating cells by microinjection

1988 ◽  
Vol 91 (2) ◽  
pp. 201-209
Author(s):  
M.G. Bergman ◽  
E. Wawra ◽  
M. Winge
Keyword(s):  
Nucleic Acid ◽  
Natural Environment ◽  
Specific Interaction ◽  
Condensed State ◽  
Pulse Labelling ◽  
Chicken Erythrocyte ◽  
Biological Functions ◽  
Proliferating Cells ◽  
Histone H5 ◽  
Transcription And Replication

Chicken erythrocyte histone H5 has been suggested repeatedly to be a general suppressor of transcription and replication. Therefore, the biological functions of H5 were investigated and compared with those of H1 (H1a + H1b) by microinjection of the purified proteins into proliferating L6 rat myoblasts. By pulse-labelling of the injected cells with [3H]uridine and [3H]thymidine it was shown that H5 blocked both transcription and replication substantially, and that the chromatin of the injected cells became densely compacted. H1 also suppressed these functions, but to a much lesser degree. The effects were specific and not caused by change in intracellular pH caused by introduction of the very basic H5, or its non-specific interaction with nucleic acid, since injection of protamine or lysozyme did not affect the cells. The migration and localization of injected H5 was monitored at different times after injection by immunofluorescence, which revealed that H5 was efficiently and stably concentrated in the nucleus. The results indicate that H5 indeed might function as an inactivator of the erythroid genome in its natural environment, probably by keeping the chromatin in a very condensed state.

Location of the globular region in chicken erythrocyte histone H5

1977 ◽  
Vol 493 (2) ◽  
pp. 283-292 ◽  
Author(s):  
Colyn Crane-Robinson ◽  
Gilbert Briand ◽  
Pierre Sautière ◽  
Madeleine Champagne
Keyword(s):  
Chicken Erythrocyte ◽  
Histone H5

scholarly journals Nucleic Acids Chemistry and Engineering: Special Issue on Nucleic Acid Conjugates for Biotechnological Applications

2021 ◽  
Vol 11 (8) ◽  
pp. 3594
Author(s):  
Tamaki Endoh ◽  
Eriks Rozners ◽  
Takashi Ohtsuki
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Genetic Information ◽  
Biotechnological Applications ◽  
Biological Functions ◽  
Primary Sequence ◽  
Special Issue

Nucleic acids not only store genetic information in their primary sequence but also exhibit biological functions through the formation of their unique structures [...]

scholarly journals Does high-mobility-group non-histone protein HMG 1 interact specifically with histone H1 subfractions?

1979 ◽  
Vol 183 (3) ◽  
pp. 657-662 ◽  
Author(s):  
P D Cary ◽  
K V Shooter ◽  
G H Goodwin ◽  
E W Johns ◽  
J Y Olayemi ◽  
...  
Keyword(s):  
Specific Interaction ◽  
High Mobility ◽  
Histone H1 ◽  
High Mobility Group ◽  
Chromosomal Protein ◽  
Histone Protein ◽  
Total Histone ◽  
Equilibrium Sedimentation ◽  
Histone H5

The interaction of the non-histone chromosomal protein HMG (high-mobility group) 1 with histone H1 subfractions was investigated by equilibrium sedimentation and n.m.r. sectroscopy. In contrast with a previous report [Smerdon & Isenberg (1976) Biochemistry 15, 4242–4247], it was found, by using equilibrium-sedimentation analysis, that protein HMG 1 binds to all three histone H1 subfractions CTL1, CTL2, and CTL3, arguing against there being a specific interaction between protein HMG 1 and only two of the subfractions, CTL1 and CTL2. Raising the ionic strength of the solutions prevents binding of protein HMG 1 to total histone H1 and the three subfractions, suggesting that the binding in vitro is simply a non-specific ionic interaction between acidic regions of the non-histone protein and the basic regions of the histone. Protein HMG 1 binds to histone H5 also, supporting this view. The above conclusions are supported by n.m.r. studies of protein HMG 1/histone H1 subfraction mixtures. When the two proteins were mixed, there was little perturbation of the n.m.r. spectra and there was no evidence for specific interaction of protein HMG 1 with any of the subfractions. It therefore remains an open question as to whether protein HMG 1 and histone H1 are complexed together in chromatin.

Chicken erythrocyte histone H5 (1980) FEBS Letters 112, 147-151

FEBS Letters ◽  
1980 ◽  
Vol 115 (2) ◽  
pp. 327-327
Author(s):  
G. Briand ◽  
D. Kmiecik ◽  
P. Sautiere ◽  
D. Wouters ◽  
O. Borie-Loy ◽  
...  
Keyword(s):  
Chicken Erythrocyte ◽  
Histone H5

Nucleic Acid Analogs: Their Specific Interaction and Applicability

1990 ◽  
pp. 253-267 ◽  
Author(s):  
Kiichi Takemoto ◽  
Eiko Mochizuki ◽  
Takehiko Wada ◽  
Yoshiaki Inaki
Keyword(s):  
Nucleic Acid ◽  
Specific Interaction ◽  
Nucleic Acid Analogs

scholarly journals The Peptidyl-prolyl Isomerase Pin1 in Neuronal Signaling: from Neurodevelopment to Neurodegeneration

2020 ◽  
Author(s):  
Francesca Fagiani ◽  
Stefano Govoni ◽  
Marco Racchi ◽  
Cristina Lanni
Keyword(s):  
Intracellular Signaling ◽  
Cell Cycle Progression ◽  
Wide Spectrum ◽  
Relevant Information ◽  
Synaptic Activity ◽  
Biological Functions ◽  
Prolyl Isomerase ◽  
Proliferating Cells ◽  
Peptidyl Prolyl Isomerase ◽  
Age Related

Abstract The peptidyl-prolyl isomerase Pin1 is a unique enzyme catalyzing the isomerization of the peptide bond between phosphorylated serine-proline or threonine-proline motifs in proteins, thereby regulating a wide spectrum of protein functions, including folding, intracellular signaling, transcription, cell cycle progression, and apoptosis. Pin1 has been reported to act as a key molecular switch inducing cell-type-specific effects, critically depending on the different phosphorylation patterns of its targets within different biological contexts. While its implication in proliferating cells, and, in particular, in the field of cancer, has been widely characterized, less is known about Pin1 biological functions in terminally differentiated and post-mitotic neurons. Notably, Pin1 is widely expressed in the central and peripheral nervous system, where it regulates a variety of neuronal processes, including neuronal development, apoptosis, and synaptic activity. However, despite studies reporting the interaction of Pin1 with neuronal substrates or its involvement in specific signaling pathways, a more comprehensive understanding of its biological functions at neuronal level is still lacking. Besides its implication in physiological processes, a growing body of evidence suggests the crucial involvement of Pin1 in aging and age-related and neurodegenerative diseases, including Alzheimer’s disease, Parkinson disease, frontotemporal dementias, Huntington disease, and amyotrophic lateral sclerosis, where it mediates profoundly different effects, ranging from neuroprotective to neurotoxic. Therefore, a more detailed understanding of Pin1 neuronal functions may provide relevant information on the consequences of Pin1 deregulation in age-related and neurodegenerative disorders.

Topography of nucleic acid helices in solution. XXVI. Specific interaction of peptides with nucleic acids

Biochemistry ◽  
1972 ◽  
Vol 11 (18) ◽  
pp. 3429-3435 ◽  
Author(s):  
Edmond J. Gabbay ◽  
Karl Sanford ◽  
C. Stuart Baxter
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acids ◽  
Specific Interaction

An analysis of the mitotic cell cycle in the root meristem of Zea mays

1973 ◽  
Vol 183 (1073) ◽  
pp. 385-398 ◽  
Keyword(s):  
Cell Cycle ◽  
Zea Mays ◽  
Root Meristem ◽  
Mitotic Cell ◽  
Mitotic Cell Cycle ◽  
Pulse Labelling ◽  
Quiescent Centre ◽  
Proliferating Cells ◽  
Average Delay ◽  
The Mean

A pulse labelling experiment was used to study the mitotic cell cycle of proliferating cells throughout the root meristem of Zea mays . Seventeen different regions were identified within the area of proliferative activity, extending from the initial cells of the cap columella up to the stele, cortex and epidermis 1000 μm from the cap-quiescent centre junction, and the data were analysed for each region separately. The analyses were made in terms of a mathematical model for cell proliferation and yield statistically efficient estimates of the cell-cycle parameters. The validity of the model is discussed in some detail. It appears that the main difference between the regions studied is in the mean duration of G 1 , that is, the average delay a newborn cell experiences before it begins to synthesize DNA. The mean durations of S and G 2 , the DNA-synthetic and post-DNA-synthetic phases of the mitotic cycle, are relatively constant. The one exception to this pattern is the quiescent centre; this region includes a relatively high proportion of slowly dividing and non-proliferating cells.

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