scholarly journals Amino Acid Exchanges in the Putative Nuclear Export Signal of Adenovirus Type 5 L4-100K Severely Reduce Viral Progeny due to Effects on Hexon Biogenesis

2012 ◽  
Vol 87 (3) ◽  
pp. 1893-1898 ◽  
Author(s):  
Orkide O. Koyuncu ◽  
Thomas Speiseder ◽  
Thomas Dobner ◽  
Melanie Schmid
Keyword(s):  
Amino Acid ◽  
Nuclear Export ◽  
Late Phase ◽  
Nuclear Export Signal ◽  
Virus Production ◽  
Adenovirus Type ◽  
Progeny Virus ◽  
Selective Translation ◽  
Adenovirus Type 5 ◽  
Export Signal

ABSTRACTThe adenovirus type 5 nonstructural L4-100K protein is indispensable for efficient lytic infection. During the late phase, L4-100K promotes selective translation of viral late transcripts and mediates the trimerization of the major capsid protein hexon. In the present study, the role of a potential nuclear export signal in L4-100K was investigated. Intriguingly, amino acid substitutions in this sequence resulted in severely diminished progeny virus production, seemingly by precluding proper hexon biogenesis.

scholarly journals The Nuclear Export Signal within the E4orf6 Protein of Adenovirus Type 5 Supports Virus Replication and Cytoplasmic Accumulation of Viral mRNA

2000 ◽  
Vol 74 (2) ◽  
pp. 764-772 ◽  
Author(s):  
Silke Weigel ◽  
Matthias Dobbelstein
Keyword(s):  
Nuclear Export ◽  
Late Phase ◽  
Nuclear Export Signal ◽  
Adenovirus Type ◽  
Adenovirus Infection ◽  
Viral Mrna ◽  
Viral Dna ◽  
Cytoplasmic Accumulation ◽  
Adenovirus Type 5 ◽  
Export Signal

ABSTRACT During the late phase of adenovirus infection, viral mRNA is efficiently transported from the nucleus to the cytoplasm while most cellular mRNA species are retained in the nucleus. Two viral proteins, E1B-55 kDa and E4orf6, are both necessary for these effects. The E4orf6 protein of adenovirus type 5 binds and relocalizes E1B-55 kDa, and the complex of the two proteins was previously shown to shuttle continuously between the nucleus and cytoplasm. Nucleocytoplasmic transport of the complex is achieved by a nuclear export signal (NES) within E4orf6. Mutation of this signal sequence severely reduces the ability of the E1B-55 kDa–E4orf6 complex to leave the nucleus. Here, we examined the role of functional domains within E4orf6 during virus infection. E4orf6 or mutants derived from it were transiently expressed, followed by infection with recombinant adenovirus lacking the E4 region and determination of virus yield. An arginine-rich putative alpha helix near the carboxy terminus of E4orf6 contributes to E1B-55 kDa binding and relocalization as well as to the synthesis of viral DNA, mRNA, and proteins. Further mutational analysis revealed that mutation of the NES within E4orf6 considerably reduces its ability to support virus production. The same effect was observed when nuclear export was blocked with a competitor. Further, a functional NES within E4orf6 contributed to the efficiency of late virus protein synthesis and viral DNA replication, as well as total and cytoplasmic accumulation of viral late mRNA. Our data support the view that NES-mediated nucleocytoplasmic shuttling strongly enhances most, if not all, intracellular activities of E4orf6 during the late phase of adenovirus infection.

scholarly journals The Adenovirus Type 5 E1B-55K Oncoprotein Actively Shuttles in Virus-Infected Cells, Whereas Transport of E4orf6 Is Mediated by a CRM1-Independent Mechanism

2001 ◽  
Vol 75 (12) ◽  
pp. 5677-5683 ◽  
Author(s):  
Tanja Dosch ◽  
Florian Horn ◽  
Grit Schneider ◽  
Friedrich Krätzer ◽  
Thomas Dobner ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Mrna Export ◽  
Nuclear Export Signal ◽  
Adenovirus Type ◽  
Alternative Mechanism ◽  
Leptomycin B ◽  
Infected Cells ◽  
Adenovirus Type 5 ◽  
Export Signal

ABSTRACT The E1B-55K and E4orf6 proteins of adenovirus type 5 are involved in viral mRNA export. Here we demonstrate that adenovirus infection does not inhibit the function of the E1B-55K nuclear export signal and that E1B-55K also shuttles in infected cells. Even during virus infection, E1B-55K was exported by the leptomycin B-sensitive CRM1 pathway, whereas E4orf6 transport appeared to be mediated by an alternative mechanism. Our results strengthen the potential role of E1B-55K as the “driving force” for adenoviral late mRNA export.

scholarly journals A TFEB nuclear export signal integrates amino acid supply and glucose availability

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Linxin Li ◽  
Hans J. Friedrichsen ◽  
Sarah Andrews ◽  
Sarah Picaud ◽  
Laurent Volpon ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Export Signal ◽  
Glucose Availability

Comparative Study on Mitogen Activated Protein Kinase of Plasmodium Species by Using in silico Method

2012 ◽  
Vol 9 (1) ◽  
pp. 1
Author(s):  
Mohd Fakharul Zaman Raja Yahya ◽  
Hasidah Mohd Sidek
Keyword(s):  
Amino Acid ◽  
In Silico ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Plasmodium Species ◽  
Mitogen Activated Protein Kinase ◽  
Multiple Sequence ◽  
Wide Range ◽  
Mitogen Activated Protein ◽  
Human Plasmodium

Malaria parasites, Plasmodium can infect a wide range of hosts including humans and rodents. There are two copies of mitogen activated protein kinases (MAPKs) in Plasmodium, namely MAPK1 and MAPK2. The MAPKs have been studied extensively in the human Plasmodium, P. falciparum. However, the MAPKs from other Plasmodium species have not been characterized and it is therefore the premise of presented study to characterize the MAPKs from other Plasmodium species-P. vivax, P. knowlesi, P. berghei, P. chabaudi and P.yoelli using a series of publicly available bioinformatic tools. In silico data indicates that all Plasmodium MAPKs are nuclear-localized and contain both a nuclear localization signal (NLS) and a Leucine-rich nuclear export signal (NES). The activation motifs of TDY and TSH were found to be fully conserved in Plasmodium MAPK1 and MAPK2, respectively. The detailed manual inspection of a multiple sequence alignment (MSA) construct revealed a total of 17 amino acid stack patterns comprising of different amino acids present in MAPKJ and MAPK2 respectively, with respect to rodent and human Plasmodia. It is proposed that these amino acid stack patterns may be useful in explaining the disparity between rodent and human Plasmodium MAPKs. 

Comparative Study on Mitogen Activated Protein Kinase of Plasmodium Species by Using In silico Method

2012 ◽  
Vol 9 (1) ◽  
pp. 1
Author(s):  
Mohd Fakharul Zaman Raja Yahya ◽  
Hasidah Mohd Sidek
Keyword(s):  
Amino Acid ◽  
In Silico ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Plasmodium Species ◽  
Mitogen Activated Protein Kinase ◽  
Multiple Sequence ◽  
Bioinformatic Tools ◽  
Wide Range ◽  
Human Plasmodium

Malaria parasites, Plasmodium can infect a wide range ofhosts including humans and rodents. There are two copies ofmitogen activated protein kinases (MAPKs) in Plasmodium, namely MAPK1 and MAPK2. The MAPKs have been studied extensively in the human Plasmodium, P. falciparum. However, the MAPKs from other Plasmodium species have not been characterized and it is therefore the premise ofpresented study to characterize the MAPKs from other Plasmodium species-P. vivax, P. knowlesi, P. berghei, P. chabaudi and P.yoelli using a series ofpublicly available bioinformatic tools. In silico data indicates that all Plasmodium MAPKs are nuclear-localizedandcontain both a nuclear localization signal (NLS) anda Leucine-rich nuclear export signal (NES). The activation motifs ofTDYand TSH werefound to befully conserved in Plasmodium MAPK1 and MAPK2, respectively. The detailed manual inspection ofa multiple sequence alignment (MSA) construct revealed a total of 17 amino acid stack patterns comprising ofdifferent amino acids present in MAPK1 and MAPK2 respectively, with respect to rodent and human Plasmodia. 1t is proposed that these amino acid stack patterns may be useful in explaining the disparity between rodent and human Plasmodium MAPKs.

The Structure of BRMS1 Nuclear Export Signal and SNX6 Interacting Region Reveals a Hexamer Formed by Antiparallel Coiled Coils

2011 ◽  
Vol 411 (5) ◽  
pp. 1114-1127 ◽  
Author(s):  
Mercedes Spínola-Amilibia ◽  
José Rivera ◽  
Miguel Ortiz-Lombardía ◽  
Antonio Romero ◽  
José L. Neira ◽  
...  
Keyword(s):  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Coiled Coils ◽  
Export Signal

scholarly journals Nuclear Export of L-Periaxin, Mediated by Its Nuclear Export Signal in the PDZ Domain

PLoS ONE ◽  
2014 ◽  
Vol 9 (3) ◽  
pp. e91953 ◽  
Author(s):  
Yawei Shi ◽  
Lei Zhang ◽  
Ting Yang
Keyword(s):  
Nuclear Export ◽  
Pdz Domain ◽  
Nuclear Export Signal ◽  
Export Signal
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