14-3-3? is a cruciform DNA binding protein and associates in vivo with origins of DNA replication

2002 ◽  
Vol 87 (2) ◽  
pp. 194-207 ◽  
Author(s):  
David Alvarez ◽  
Olivia Novac ◽  
Mario Callejo ◽  
Marcia T. Ruiz ◽  
Gerald B. Price ◽  
...  
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Cruciform Dna

scholarly journals In Vivo Occupancy of Mitochondrial Single-Stranded DNA Binding Protein Supports the Strand Displacement Mode of DNA Replication

PLoS Genetics ◽  
2014 ◽  
Vol 10 (12) ◽  
pp. e1004832 ◽  
Author(s):  
Javier Miralles Fusté ◽  
Yonghong Shi ◽  
Sjoerd Wanrooij ◽  
Xuefeng Zhu ◽  
Elisabeth Jemt ◽  
...  
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Strand Displacement ◽  
Single Stranded Dna ◽  
Displacement Mode

scholarly journals The DNA-binding protein HTa from Thermoplasma acidophilum is an archaeal histone analog

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Antoine Hocher ◽  
Maria Rojec ◽  
Jacob B Swadling ◽  
Alexander Esin ◽  
Tobias Warnecke
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Coli Strain ◽  
Micrococcal Nuclease ◽  
Thermoplasma Acidophilum ◽  
Chromatin Architecture ◽  
Archaeal Histone

Histones are a principal constituent of chromatin in eukaryotes and fundamental to our understanding of eukaryotic gene regulation. In archaea, histones are widespread but not universal: several lineages have lost histone genes. What prompted or facilitated these losses and how archaea without histones organize their chromatin remains largely unknown. Here, we elucidate primary chromatin architecture in an archaeon without histones, Thermoplasma acidophilum, which harbors a HU family protein (HTa) that protects part of the genome from micrococcal nuclease digestion. Charting HTa-based chromatin architecture in vitro, in vivo and in an HTa-expressing E. coli strain, we present evidence that HTa is an archaeal histone analog. HTa preferentially binds to GC-rich sequences, exhibits invariant positioning throughout the growth cycle, and shows archaeal histone-like oligomerization behavior. Our results suggest that HTa, a DNA-binding protein of bacterial origin, has converged onto an architectural role filled by histones in other archaea.

scholarly journals Gene D5 product of bacteriophage T5: DNA-binding protein affecting DNA replication and late gene expression.

1979 ◽  
Vol 29 (1) ◽  
pp. 322-327 ◽  
Author(s):  
D J McCorquodale ◽  
J Gossling ◽  
R Benzinger ◽  
R Chesney ◽  
L Lawhorne ◽  
...  
Keyword(s):  
Gene Expression ◽  
Dna Replication ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Late Gene ◽  
Late Gene Expression ◽  
Bacteriophage T5

scholarly journals Nuclear localization of herpesvirus proteins: potential role for the cellular framework.

1983 ◽  
Vol 3 (3) ◽  
pp. 315-324 ◽  
Author(s):  
M P Quinlan ◽  
D M Knipe
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Capsid Protein ◽  
Cell Nucleus ◽  
Binding Protein ◽  
Cell Monolayer ◽  
Dna Binding Protein ◽  
Actual State ◽  
Viral Dna ◽  
Viral Dna Replication

Two herpes simplex virus proteins, the major capsid protein and the major DNA binding protein, are specifically localized to the nucleus of infected cells. We have found that the major proportion of these proteins is associated with the detergent-insoluble matrix or cytoskeletal framework of the infected cell from the time of their synthesis until they have matured to their final binding site in the cell nucleus. These results suggest that these two proteins may interact with or bind to the cellular cytoskeleton during or soon after their synthesis and throughout transport into the cell nucleus. In addition, the DNA binding protein remains associated with the nuclear skeleton at times when it is bound to viral DNA. Thus, viral DNA may also be attached to the nuclear framework. We have demonstrated that the DNA binding protein and the capsid protein exchange from the cytoplasmic framework to the nuclear framework, suggesting the direct movement of the proteins from one structure to the other. Inhibition of viral DNA replication enhanced the binding of the DNA binding protein to the cytoskeleton and increased the rate of exchange from the cytoplasmic framework to the nuclear framework, suggesting a functional relationship between these events. Inhibition of viral DNA replication resulted in decreased synthesis and transport of the capsid protein. We have been unable to detect any artificial binding of these proteins to the cytoskeleton when solubilized viral proteins were mixed with a cytoskeletal fraction or a cell monolayer. This suggested that the attachment of these proteins to the cytoskeleton represents the actual state of these proteins within the cell.

Nuclear localization of herpesvirus proteins: potential role for the cellular framework

1983 ◽  
Vol 3 (3) ◽  
pp. 315-324
Author(s):  
M P Quinlan ◽  
D M Knipe
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Capsid Protein ◽  
Cell Nucleus ◽  
Binding Protein ◽  
Cell Monolayer ◽  
Dna Binding Protein ◽  
Actual State ◽  
Viral Dna ◽  
Viral Dna Replication

Two herpes simplex virus proteins, the major capsid protein and the major DNA binding protein, are specifically localized to the nucleus of infected cells. We have found that the major proportion of these proteins is associated with the detergent-insoluble matrix or cytoskeletal framework of the infected cell from the time of their synthesis until they have matured to their final binding site in the cell nucleus. These results suggest that these two proteins may interact with or bind to the cellular cytoskeleton during or soon after their synthesis and throughout transport into the cell nucleus. In addition, the DNA binding protein remains associated with the nuclear skeleton at times when it is bound to viral DNA. Thus, viral DNA may also be attached to the nuclear framework. We have demonstrated that the DNA binding protein and the capsid protein exchange from the cytoplasmic framework to the nuclear framework, suggesting the direct movement of the proteins from one structure to the other. Inhibition of viral DNA replication enhanced the binding of the DNA binding protein to the cytoskeleton and increased the rate of exchange from the cytoplasmic framework to the nuclear framework, suggesting a functional relationship between these events. Inhibition of viral DNA replication resulted in decreased synthesis and transport of the capsid protein. We have been unable to detect any artificial binding of these proteins to the cytoskeleton when solubilized viral proteins were mixed with a cytoskeletal fraction or a cell monolayer. This suggested that the attachment of these proteins to the cytoskeleton represents the actual state of these proteins within the cell.

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