HBx Protein of Hepatitis B Virus Promotes Reinitiation of DNA Replication by Regulating Expression and Intracellular Stability of Replication Licensing Factor CDC6

Pandey, Vijaya; Kumar, Vijay

doi:10.1074/jbc.m112.359760

Cited by 19 publications

(23 citation statements)

References 47 publications

(51 reference statements)

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“…The beads were washed three times with chilled NaCl/Pi, resuspended in laemmli buffer, boiled for 10 min and the beads were spin down. Supernatants were subjected to western blotting .…”

Section: Methodsmentioning

confidence: 99%

Influenza A viral nucleoprotein interacts with cytoskeleton scaffolding protein α‐actinin‐4 for viral replication

et al. 2014

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Influenza A virus (IAV), similar to other viruses, exploits the machinery of human host cells for its survival and replication. We identified a-actinin-4, a host cytoskeletal protein, as an interacting partner of IAV nucleoprotein (NP). We confirmed this interaction using co-immunoprecipitation studies, first in a coupled in vitro transcription-translation assay and then in cells either transiently co-expressing the two proteins or infected with whole IAV. Importantly, the NP-actinin-4 interaction was observed in several IAV subtypes, including the 2009 H1N1 pandemic virus. Moreover, immunofluorescence studies revealed that both NP and actinin-4 co-localized largely around the nucleus and also in the cytoplasmic region of virus-infected A549 cells. Silencing of actinin-4 expression resulted in not only a significant decrease in NP, M2 and NS1 viral protein expression, but also a reduction of both NP mRNA and viral RNA levels, as well as viral titers, 24 h post-infection with IAV, suggesting that actinin-4 was critical for viral replication. Furthermore, actinin-4 depletion reduced the amount of NP localized in the nucleus. Treatment of infected cells with wortmannin, a known inhibitor of actinin-4, led to a decrease in NP mRNA levels and also caused the nuclear retention of NP, further strengthening our previous observations. Taken together, the results of the present study indicate that actinin-4, a novel interacting partner of IAV NP, plays a crucial role in viral replication and this interaction may participate in nuclear localization of NP and/or viral ribonucleoproteins.

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“…The beads were washed three times with chilled NaCl/Pi, resuspended in laemmli buffer, boiled for 10 min and the beads were spin down. Supernatants were subjected to western blotting .…”

Section: Methodsmentioning

confidence: 99%

Influenza A viral nucleoprotein interacts with cytoskeleton scaffolding protein α‐actinin‐4 for viral replication

et al. 2014

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“…Cell cycle analysis was performed as described previously . Briefly, cells were washed with NaCl/P i (×1), fixed in 70% ethanol and stained with propidium iodide (50 mg·mL –1 ).…”

Section: Methodsmentioning

confidence: 99%

Combinatorial action of transcription factors orchestrates cell cycle‐dependent expression of the ribosomal protein genes and ribosome biogenesis

2014

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Nucleolar assembly begins at the early G1 phase of the cell cycle and is a hub of ribosomal DNA transcription and rRNA biosynthesis. The newlyformed rRNAs together with ribosomal proteins (RPs) constitute the building block of the ribosomal machinery. Although RPs play a major role in protein biosynthesis, their own regulation and expression is rather poorly understood. In the present study, we investigated the regulation of RP genes RPS27a, RPS24, RPS6, RPL9 and RPL4 in synchronized mammalian cell culture. Quantitative RT-PCR analysis indicated their expression during the mid to late G1 phase, whereas the rRNA genes were expressed during the early G1 phase of the cell cycle. The promoter reporter analysis of the RPS27a gene revealed that it could be synergistically stimulated by the transcription factors specificity protein 1 (Sp1) and cAMP response element-binding protein (CREB). However, E2F transcription factor 1 (E2F1) appeared to negatively regulate gene expression. Chromatin immunoprecipitation studies confirmed the promoter occupancy of Sp1, CREB and E2F1. Although Sp1 and CREB binding enhanced the promoter occupancy of histone acetyltransferases PCAF, p300 and CREB binding protein, E2F1 facilitated the recruitment of histone deacetylases. Both acetylation (histone H4 pan-acetyl, histone H3 acetyl Lys 14) and methylation (histone H3 trimethyl Lys 9) marks were observed in the RPS27a promoter region, suggesting their important regulatory role in gene expression. Because the promoter regions of most RP genes are well conserved, we propose that their orchestrated regulation and synthesis during the cell cycle facilitates ribosome biogenesis.

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“…Cell cycle analysis was performed as described previously (Mukherji et al, 2007;Pandey and Kumar, 2012). Briefly, cells were washed with PBS (1×), fixed in 70% ethanol, and stained with propidium iodide (50 mg/ml).…”

Section: Cell Synchronization and Cell Cycle Analysismentioning

confidence: 99%

“…ChIP assay was carried out as described earlier (Pandey and Kumar, 2012). Briefly, IHH cells were cross-linked with formaldehyde (1%), lysed, and sonicated over ice (7 pulses at 30% amplitude) and centrifuged at 13,000 rpm for 10 min to obtain the supernatant.…”

Section: Chromatin Immunoprecipitation (Chip) Assaymentioning

confidence: 99%

DNA damage stress induces the expression of Ribosomal Protein S27a gene in a p53-dependent manner

Nosrati

Kapoor

Kumar

2015

Gene

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HBx Protein of Hepatitis B Virus Promotes Reinitiation of DNA Replication by Regulating Expression and Intracellular Stability of Replication Licensing Factor CDC6

Cited by 19 publications

References 47 publications

Influenza A viral nucleoprotein interacts with cytoskeleton scaffolding protein α‐actinin‐4 for viral replication

Influenza A viral nucleoprotein interacts with cytoskeleton scaffolding protein α‐actinin‐4 for viral replication

Combinatorial action of transcription factors orchestrates cell cycle‐dependent expression of the ribosomal protein genes and ribosome biogenesis

DNA damage stress induces the expression of Ribosomal Protein S27a gene in a p53-dependent manner

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