The histone-like C-terminal extension in ribosomal protein S6 in Aedes and Anopheles mosquitoes is encoded within the distal portion of exon 3

Hernandez, Vida P.; Higgins, LeeAnn; Schwientek, Melinda Sue; Fallon, Ann M.

doi:10.1016/s0965-1748(03)00095-x

Cited by 10 publications

(16 citation statements)

References 38 publications

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“…The RpS6 present in mosquitoes contains a unique C-terminal tail (19,20), suggesting that RpS6 plays an altered role in the mosquito ribosome. Although alphaviruses have a dramatically different effect on host translation in mosquito cells and mosquito RpS6 is divergent, nsP2 is able to associate with mosquito RpS6.…”

Section: Discussionmentioning

confidence: 99%

“…VEE nsP2 associates with RpS6 from mosquitoes. Although eukaryotic RpS6 is well conserved, in Aedes and Anopheles mosquitoes there is a unique C-terminal extension on RpS6 (19,20). This ϳ100-amino-acid tail is located immediately downstream of the cluster of serine residues on RpS6 that are the sites of phosphorylation.…”

Section: Vol 80 2006 Association Of Rps6 With Nonstructural Proteinmentioning

confidence: 99%

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Ribosomal Protein S6 Associates with Alphavirus Nonstructural Protein 2 and Mediates Expression from Alphavirus Messages

Montgomery

Berglund

Beard

et al. 2006

J Virol

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Although alphaviruses dramatically alter cellular function within hours of infection, interactions between alphaviruses and specific host cellular proteins are poorly understood. Although the alphavirus nonstructural protein 2 (nsP2) is an essential component of the viral replication complex, it also has critical auxiliary functions that determine the outcome of infection in the host. To gain a better understanding of nsP2 function, we sought to identify cellular proteins with which Venezuelan equine encephalitis virus nsP2 interacted. We demonstrate here that nsP2 associates with ribosomal protein S6 (RpS6) and that nsP2 is present in the ribosome-containing fractions of a polysome gradient, suggesting that nsP2 associates with RpS6 in the context of the whole ribosome. This result was noteworthy, since viral replicase proteins have seldom been described in direct association with components of the ribosome. The association of RpS6 with nsP2 was detected throughout the course of infection, and neither the synthesis of the viral structural proteins nor the presence of the other nonstructural proteins was required for RpS6 interaction with nsP2. nsP1 also was associated with RpS6, but other nonstructural proteins were not. RpS6 phosphorylation was dramatically diminished within hours after infection with alphaviruses. Furthermore, a reduction in the level of RpS6 protein expression led to diminished expression from alphavirus subgenomic messages, whereas no dramatic diminution in cellular translation was observed. Taken together, these data suggest that alphaviruses alter the ribosome during infection and that this alteration may contribute to differential translation of host and viral messages.The Alphavirus genus contains over 25 recognized viruses with a wide geographic distribution. Venezuelan equine encephalitis virus (VEE) is a New World alphavirus that is maintained in nature by cycling between a mosquito vector and susceptible vertebrate hosts. VEE is responsible for periodic outbreaks of disease in humans and equines and is classified as a select agent, making it a prominent pathogen among the alphaviruses.Alphaviruses possess a genome of single-stranded messagesense RNA that is approximately 11.5 kb in length. The alphavirus genome is organized such that the 5Ј two-thirds of the genome encodes four nonstructural proteins (nsP1 through nsP4), whereas the 3Ј one-third encodes three mature structural proteins (capsid, E2, and E1) that are expressed at high levels after transcription from an internal 26S subgenomic mRNA promoter. The viral genome appears to be similar to cellular mRNAs, since it contains 5Ј and 3Ј untranslated regions, with a 5Ј-terminal methylguanylate cap and a 3Ј-terminal polyadenylate tail. Upon release into a host cell, the viral genomic RNA is directly translated by the cellular translation machinery. The nonstructural proteins are synthesized as two polyproteins, termed P123 and P1234. P123 results when translation terminates at an opal termination codon between nsP3 and nsP4. When t...

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Section: Discussionmentioning

confidence: 99%

Section: Vol 80 2006 Association Of Rps6 With Nonstructural Proteinmentioning

confidence: 99%

Ribosomal Protein S6 Associates with Alphavirus Nonstructural Protein 2 and Mediates Expression from Alphavirus Messages

Montgomery

Berglund

Beard

et al. 2006

J Virol

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“…Mosquito PCR primers were based on the single-copy gene for ribosomal protein RpS6 (Hernandez et al 2003), which has unusual variation among mosquito species (Fallon and Li 2007). Wolbachia primers were based on ribosomal proteins rpS12 (rpsL) and rpS7 (rpsG), which are members of the "str operon" in Escherichia coli (Saito et al 1994), and whose gene order is conserved in the genome of Drosophila melanogaster wMel (Wu et al 2004).…”

Section: Dna Extraction and Pcr Analysesmentioning

confidence: 99%

Cytological properties of an Aedes albopictus mosquito cell line infected with Wolbachia strain wAlbB

Fallon

2008

In Vitro Cell.Dev.Biol.-Animal

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In vitro production of the obligate intracellular bacterium, Wolbachia pipientis, is essential to its manipulation as a genetic tool to spread transgenes within vector populations. We have adapted the Wolbachia-infected Aa23 Aedes albopictus mosquito cell line to Eagle's minimal medium, supplemented with nonessential amino acids, glutamine, and 20% fetal bovine serum. When plated at low densities, Aa23E cells grew as patchy monolayers, comprised of non-contiguous clusters of cells that gave rise to solid clumps of tightly adherent cells. Multicellular clumps eventually detached from the substrate and floated freely in the medium. Removal of Wolbachia by treatment with tetracycline did not alter the cytological properties of the host cells, which had a population doubling time of 4-5 d. The presence of Wolbachia was monitored by Giemsa staining of cytological preparations, polymerase chain reaction (PCR) amplification of Wolbachia 16S ribosomal DNA, and by simultaneous PCR amplification of ribosomal protein genes from Wolbachia and mosquito host cell genomes. Wolbachia morphology was pleomorphic, and Wolbachia DNA persisted in the culture medium for several weeks after degradation of PCR-amplifiable host cell DNA.

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“…We have recently shown that RPS6 protein isolated from ribosomal subunits retains its histone H1-like tail [4]. Thus, unlike the case with the ubiquitinated ribosomal protein S27a in the rat [5], the histone tail is not removed from the mosquito ribosomal protein prior to ribosome assembly.…”

Section: Introductionmentioning

confidence: 99%

“…In both Aedes and Anopheles mosquitoes, the C-terminal extension was completely encoded in Exon 3, directly contiguous with upstream open reading frame encoding the series of serines that may be phosphorylated [4]. Anopheline mosquitoes are believed to be ancestral to the Culicidae, which includes the genera Aedes and Culex [6].…”

Section: Introductionmentioning

confidence: 99%

PCR cloning of a histone H1 gene from Anopheles stephensi mosquito cells: comparison of the protein sequence with histone H1-like, C-terminal extensions on mosquito ribosomal protein S6

Zhai

Fallon

2005

BMC Genomics

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The histone-like C-terminal extension in ribosomal protein S6 in Aedes and Anopheles mosquitoes is encoded within the distal portion of exon 3

Cited by 10 publications

References 38 publications

Ribosomal Protein S6 Associates with Alphavirus Nonstructural Protein 2 and Mediates Expression from Alphavirus Messages

Ribosomal Protein S6 Associates with Alphavirus Nonstructural Protein 2 and Mediates Expression from Alphavirus Messages

Cytological properties of an Aedes albopictus mosquito cell line infected with Wolbachia strain wAlbB

PCR cloning of a histone H1 gene from Anopheles stephensi mosquito cells: comparison of the protein sequence with histone H1-like, C-terminal extensions on mosquito ribosomal protein S6

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