scholarly journals Protein–protein interactions among the structural proteins of Chilo iridescent virus

2018 ◽  
Vol 99 (6) ◽  
pp. 851-859 ◽  
Author(s):  
Emine Ozsahin ◽  
Monique M. van Oers ◽  
Remziye Nalcacioglu ◽  
Zihni Demirbag
Keyword(s):  
Protein Interactions ◽  
Structural Proteins ◽  
Chilo Iridescent Virus ◽  
Protein Protein Interactions ◽  
Iridescent Virus

CIV, An Iridovirus With a Pseudo T=147 Capsid Structure

1999 ◽  
Vol 5 (S2) ◽  
pp. 1134-1135
Author(s):  
X. Yan ◽  
N. H. Olson ◽  
M. Bergoin ◽  
M. G. Rossmann ◽  
T. S. Baker
Keyword(s):  
Stem Borer ◽  
Control Agent ◽  
Structural Proteins ◽  
Chilo Iridescent Virus ◽  
Iridescent Virus ◽  
Insect Order ◽  
Rice Stem Borer ◽  
Sds Page ◽  
The Family ◽  
Potential Pest

Chilo iridescent virus (CIV), the type species of the genus Iridovirusin the family Iridoviridae,was first isolated from the rice stem borer, Chilo suppressalis,a member of Lepidoptera insect order. ‘2 CIV is being considered as a potential pest control agent because of its wide host range which includes leafhoppers and some arthropods. The virion (∼lxl09 daltons) encapsidates a 209 kbp, dsDNA genome within its fiber-covered, icosahedral shell. The virion is composed of about 26 structural proteins, two (P50 and P'50, 50kDa each) of which are the major capsid proteins. P50 migrates as a monomer in either a reducing or non-reducing SDS-PAGE gel and is exposed to the surface, whereas P'50 exists as a disulfide-bond, stabilized trimer in a non-reducing gel and is only partially exposed. Virions contain 9% lipid present as a lipid bilayer within the protein capsid.

scholarly journals The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development

2016 ◽  
Author(s):  
Markéta Kostrouchová ◽  
David Kostrouch ◽  
Ahmed A Chughtai ◽  
Filip Kaššák ◽  
Jan P. Novotný ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Protein Interactions ◽  
Structural Proteins ◽  
Mediator Complex ◽  
Cytoplasmic Localization ◽  
Protein Protein Interactions ◽  
C Elegans ◽  
Evolutionarily Conserved ◽  
Nuclear Events ◽  
Bona Fide

The evolutionarily conserved Mediator complex is a critical player in regulating transcription. Comprised of approximately two dozen proteins, Mediator integrates diverse regulatory signals through direct protein-protein interactions that, in turn, modulate the influence of Mediator on RNA Polymerase II activity. One Mediator subunit, MED28, is known to interact with cytoplasmic structural proteins, providing a potential direct link between cytoplasmic dynamics and the control of gene transcription. Although identified in many animals and plants, MED28 is not present in yeast; no bona fide MED28 has been described previously in C. elegans. Here, we identify bioinformatically F28F8.5, an uncharacterized predicted protein, as the nematode homologue of MED28. As in other metazoa, F28F8.5 has dual nuclear and cytoplasmic localization and plays critical roles in the regulation of development. F28F8.5 is a vital gene and its null mutants have severely malformed gonads and do not reproduce. Our results indicate that F28F8.5 is a homologue of MED28 and suggest that the potential to link cytoplasmic and nuclear events is conserved between MED28 vertebrate and nematode homologues.

scholarly journals Efficient Incorporation of Tegument Proteins pUL46, pUL49, and pUS3 into Pseudorabies Virus Particles Depends on the Presence of pUL21

2006 ◽  
Vol 81 (2) ◽  
pp. 1048-1051 ◽  
Author(s):  
Kathrin Michael ◽  
Barbara G. Klupp ◽  
Axel Karger ◽  
Thomas C. Mettenleiter
Keyword(s):  
Virus Particle ◽  
Protein Interactions ◽  
Pseudorabies Virus ◽  
Structural Proteins ◽  
Tegument Protein ◽  
Wild Type ◽  
Protein Protein Interactions ◽  
Virus Particles ◽  
Tegument Proteins ◽  
Drastic Decrease

ABSTRACT The mature virion of the alphaherpesvirus pseudorabies virus (PrV) contains a minimum of 31 structural proteins which are recruited into the virus particle by a network of protein-protein interactions which is only incompletely understood. We show here that deletion of the tegument protein pUL21 resulted in a drastic decrease in the incorporation of the pUL46, pUL49, and pUS3 tegument components into mature virions. Moreover, the attenuated PrV strain Bartha (PrV-Ba), which, among other defects, carries mutations in pUL21, also fails to package pUL46, pUL49, and pUS3 efficiently. By the reconstitution of wild-type pUL21 expression to PrV-Ba and the transfer of mutated PrV-Ba pUL21 into wild-type PrV, we demonstrate that this phenotype is due to the mutated pUL21.

scholarly journals Linkage map of protein–protein interactions of Porcine teschovirus

2005 ◽  
Vol 86 (10) ◽  
pp. 2763-2768 ◽  
Author(s):  
Roland Zell ◽  
Simone Seitz ◽  
Andreas Henke ◽  
Thomas Munder ◽  
Peter Wutzler
Keyword(s):  
Linkage Map ◽  
Protein Interactions ◽  
Structural Proteins ◽  
Protein Protein Interactions ◽  
Yeast Two Hybrid ◽  
Protein L ◽  
Leader Protein ◽  
Porcine Teschovirus ◽  
Two Hybrid

A yeast two-hybrid study was conducted to catalogue the protein–protein interactions of the Porcine teschovirus non-structural proteins. Five homodimer, three reciprocal heterodimer and four unidirectional heterodimer interactions were observed. While several interactions are similar to those described in previous studies using enteroviruses, such as homo- and heterodimeric interactions of the 2B, 3CD and 3D proteins, several were not found previously. Among these is the binding of the leader protein L to the proteinases 3C and 3CD. Unlike the poliovirus 3C, the teschovirus 3C proteinase dimerizes and interacts with 2BC, 3CD and 3D. The strongest interactions were observed for L–3C, L–3CD and 3C–3CD.

scholarly journals The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development

2016 ◽  
Author(s):  
Markéta Kostrouchová ◽  
David Kostrouch ◽  
Ahmed A Chughtai ◽  
Filip Kaššák ◽  
Jan P. Novotný ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Protein Interactions ◽  
Structural Proteins ◽  
Mediator Complex ◽  
Cytoplasmic Localization ◽  
Protein Protein Interactions ◽  
C Elegans ◽  
Evolutionarily Conserved ◽  
Nuclear Events ◽  
Bona Fide

The evolutionarily conserved Mediator complex is a critical player in regulating transcription. Comprised of approximately two dozen proteins, Mediator integrates diverse regulatory signals through direct protein-protein interactions that, in turn, modulate the influence of Mediator on RNA Polymerase II activity. One Mediator subunit, MED28, is known to interact with cytoplasmic structural proteins, providing a potential direct link between cytoplasmic dynamics and the control of gene transcription. Although identified in many animals and plants, MED28 is not present in yeast; no bona fide MED28 has been described previously in C. elegans. Here, we identify bioinformatically F28F8.5, an uncharacterized predicted protein, as the nematode homologue of MED28. As in other metazoa, F28F8.5 has dual nuclear and cytoplasmic localization and plays critical roles in the regulation of development. F28F8.5 is a vital gene and its null mutants have severely malformed gonads and do not reproduce. Our results indicate that F28F8.5 is a homologue of MED28 and suggest that the potential to link cytoplasmic and nuclear events is conserved between MED28 vertebrate and nematode homologues.

scholarly journals The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator ofC. elegansdevelopment

PeerJ ◽  
2017 ◽  
Vol 5 ◽  
pp. e3390
Author(s):  
Markéta Kostrouchová ◽  
David Kostrouch ◽  
Ahmed A. Chughtai ◽  
Filip Kaššák ◽  
Jan P. Novotný ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Protein Interactions ◽  
Structural Proteins ◽  
Mediator Complex ◽  
Cytoplasmic Localization ◽  
Protein Protein Interactions ◽  
Evolutionarily Conserved ◽  
Nuclear Events ◽  
Bona Fide ◽  
Null Mutants

The evolutionarily conserved Mediator complex is a critical player in regulating transcription. Comprised of approximately two dozen proteins, the Mediator integrates diverse regulatory signals through direct protein-protein interactions that, in turn, modulate the influence of Mediator on RNA Polymerase II activity. One Mediator subunit, MED28, is known to interact with cytoplasmic structural proteins, providing a potential direct link between cytoplasmic dynamics and the control of gene transcription. Although identified in many animals and plants, MED28 is not present in yeast; no bona fide MED28 has been described previously inCaenorhabditis elegans.Here, we identify bioinformatically F28F8.5, an uncharacterized predicted protein, as the nematode homologue of MED28. As in other Metazoa, F28F8.5 has dual nuclear and cytoplasmic localization and plays critical roles in the regulation of development.F28F8.5is a vital gene and its null mutants have severely malformed gonads and do not reproduce. F28F8.5 interacts on the protein level with the Mediator subunits MDT-6 and MDT-30. Our results indicate that F28F8.5 is an orthologue of MED28 and suggest that the potential to link cytoplasmic and nuclear events is conserved between MED28 vertebrate and nematode orthologues.

scholarly journals The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development

2016 ◽  
Author(s):  
Markéta Kostrouchová ◽  
David Kostrouch ◽  
Ahmed A Chughtai ◽  
Filip Kaššák ◽  
Jan P. Novotný ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Protein Interactions ◽  
Structural Proteins ◽  
Mediator Complex ◽  
Cytoplasmic Localization ◽  
Protein Protein Interactions ◽  
C Elegans ◽  
Evolutionarily Conserved ◽  
Nuclear Events ◽  
Bona Fide

The evolutionarily conserved Mediator complex is a critical player in regulating transcription. Comprised of approximately two dozen proteins, Mediator integrates diverse regulatory signals through direct protein-protein interactions that, in turn, modulate the influence of Mediator on RNA Polymerase II activity. One Mediator subunit, MED28, is known to interact with cytoplasmic structural proteins, providing a potential direct link between cytoplasmic dynamics and the control of gene transcription. Although identified in many animals and plants, MED28 is not present in yeast; no bona fide MED28 has been described previously in C. elegans. Here, we identify bioinformatically F28F8.5, an uncharacterized predicted protein, as the nematode homologue of MED28. As in other metazoa, F28F8.5 has dual nuclear and cytoplasmic localization and plays critical roles in the regulation of development. F28F8.5 is a vital gene and its null mutants have severely malformed gonads and do not reproduce. Our results indicate that F28F8.5 is a homologue of MED28 and suggest that the potential to link cytoplasmic and nuclear events is conserved between MED28 vertebrate and nematode homologues.

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