Nucleolar Protein B23 Stimulates Nuclear Import of the HIV-1 Rev Protein and NLS-Conjugated Albumin†

Biochemistry ◽  
1997 ◽  
Vol 36 (13) ◽  
pp. 3941-3949 ◽  
Author(s):  
Attila Szebeni ◽  
Bam Mehrotra ◽  
Amy Baumann ◽  
Stephen A. Adam ◽  
Paul T. Wingfield ◽  
...  
Keyword(s):  
Nuclear Import ◽  
Nucleolar Protein ◽  
Protein B23 ◽  
Hiv 1 ◽  
Rev Protein

The roles of nucleolar structure and function in the subcellular location of the HIV-1 Rev protein

1995 ◽  
Vol 108 (8) ◽  
pp. 2811-2823 ◽  
Author(s):  
M. Dundr ◽  
G.H. Leno ◽  
M.L. Hammarskjold ◽  
D. Rekosh ◽  
C. Helga-Maria ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Critical Role ◽  
Regulation Of Expression ◽  
Rna Transcription ◽  
Nucleolar Structure ◽  
Class 1 ◽  
Protein B23 ◽  
Hiv 1 ◽  
Rev Protein

The human immunodeficiency virus 1 (HIV-1) Rev transactivator protein plays a critical role in the regulation of expression of structural proteins by controlling the pathway of mRNA transport. The Rev protein is located predominantly in the nucleoli of HIV-1 infected or Rev-expressing cells. Previous studies demonstrated that the Rev protein forms a specific complex in vitro with protein B23 which is suggested to be a nucleolar receptor and/or carrier for the Rev protein. To study the role of the nucleolus and nucleolar proteins in Rev function, transfected COS-7 or transformed CMT3 cells expressing the Rev protein were examined for subcellular locations of Rev and other proteins using indirect immunofluorescence and immunoelectron microscopy. One day after transfection the Rev protein was found in most cells only in the nucleolar dense fibrillar and granular components where it colocalized with protein B23. These were designated class 1 cells. In a second class of cells Rev and B23 accumulated in the nucleoplasm as well as in nucleoli. Treatment of class 1 cells with actinomycin D (AMD) under conditions that blocked only RNA polymerase I transcription caused Rev to completely redistribute from nucleoli to the cytoplasm. Simultaneously, protein B23 was partially released from nucleoli, mostly into the nucleoplasm, with detectable amounts in the cytoplasm. In cells recovering from AMD treatment in the presence of cycloheximide Rev and B23 showed coincident relocation to nucleoli. Class 2 cells were resistant to AMD-induced Rev redistribution. Selective inhibition of RNA polymerase II transcription by alpha-amanitin or by DRB did not cause Rev to be released into the cytoplasm suggesting that active preribosomal RNA transcription is required for the nucleolar location of Rev. However, treatment with either of the latter two drugs at higher doses and for longer times caused partial disruption of nucleoli accompanied by translocation of the Rev protein to the cytoplasm. These results suggest that the nucleolar location of Rev depends on continuous preribosomal RNA transcription and a substantially intact nucleolar structure.

Location of the HIV-1 Rev protein during mitosis: inactivation of the nuclear export signal alters the pathway for postmitotic reentry into nucleoli

1996 ◽  
Vol 109 (9) ◽  
pp. 2239-2251 ◽  
Author(s):  
M. Dundr ◽  
G.H. Leno ◽  
N. Lewis ◽  
D. Rekosh ◽  
M.L. Hammarskjoid ◽  
...  
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Export ◽  
Nuclear Export Signal ◽  
Nucleolar Protein ◽  
Early Prophase ◽  
Nucleolar Proteins ◽  
Late Telophase ◽  
Export Signal ◽  
Hiv 1 ◽  
Rev Protein

The HIV-1 Rev protein localizes predominantly to the nucleolus of HIV-1-infected or Rev-expressing cells. The subcellular location of Rev during mitotic nucleolar disintegration was examined at various stages of mitosis in synchronized Rev-expressing CMT3 cells. During early prophase Rev was predominantly located in disintegrating nucleoli and began to accumulate at the peripheral regions of chromosomes in late prophase, eventually distributing uniformly on all chromosomes in prometaphase. In anaphase Rev remained associated with the perichromosomal regions, but significant amounts of Rev were also seen in numerous nucleolus-derived foci. The movement of Rev from disintegrating nucleoli to perichromosomal regions and foci was similar to that of nonribosomal nucleolar proteins, including fibrillarin, nucleolin, protein B23 and p52 of the granular component. During telophase Rev remained associated with perichromosomal regions and mitotic foci until the nuclear envelope started to reform. When nuclear envelope formation was complete in late telophase, nonribosomal nucleolar proteins were present in prenucleolar bodies (PNBs) which were eventually incorporated into nucleoli; at the same time, Rev was excluded from nuclei. In contrast, a trans-dominant negative Rev protein containing an inactive nuclear export signal reentered nuclei by the nonribosomal nucleolar protein pathway in late telophase, associating with PNBs and reformed nucleoli. Rev protein reentry into postmitotic nuclei was delayed until early G1 phase, but before the arrival of ribosomal protein S6. Thus, Rev behaves like a nonribosomal nucleolar protein through mitosis until early telophase; however, its nuclear reentry seems to require reestablishment of both a nuclear import system and active nucleoli.

HIV-1 nuclear import: in search of a leader; update 1999

1999 ◽  
Vol 4 (1-3) ◽  
pp. d772 ◽  
Author(s):  
Michael, I. Bukrinsky
Keyword(s):  
Nuclear Import ◽  
Hiv 1

scholarly journals Microbial Natural Product Alternariol 5-O-Methyl Ether Inhibits HIV-1 Integration by Blocking Nuclear Import of the Pre-Integration Complex

Viruses ◽  
2017 ◽  
Vol 9 (5) ◽  
pp. 105 ◽  
Author(s):  
Jiwei Ding ◽  
Jianyuan Zhao ◽  
Zhijun Yang ◽  
Ling Ma ◽  
Zeyun Mi ◽  
...  
Keyword(s):  
Natural Product ◽  
Methyl Ether ◽  
Nuclear Import ◽  
Hiv 1

Sequence of a phosphorylation site in nucleolar protein B23

1981 ◽  
Vol 667 (1) ◽  
pp. 209-212 ◽  
Author(s):  
Chris E. Jones ◽  
Harris Busch ◽  
Mark O.J. Olson
Keyword(s):  
Phosphorylation Site ◽  
Nucleolar Protein ◽  
Protein B23

scholarly journals Protein NPM3 Interacts with the Multifunctional Nucleolar Protein B23/Nucleophosmin and Inhibits Ribosome Biogenesis

2004 ◽  
Vol 280 (7) ◽  
pp. 5496-5502 ◽  
Author(s):  
Nian Huang ◽  
Sandeep Negi ◽  
Attila Szebeni ◽  
Mark O. J. Olson
Keyword(s):  
Ribosome Biogenesis ◽  
Nucleolar Protein ◽  
Protein B23

scholarly journals Characterization of Antiviral Activity of Benzamide Derivative AH0109 against HIV-1 Infection

2013 ◽  
Vol 57 (8) ◽  
pp. 3547-3554 ◽  
Author(s):  
Liyu Chen ◽  
Zhujun Ao ◽  
Kallesh Danappa Jayappa ◽  
Gary Kobinger ◽  
ShuiPing Liu ◽  
...  
Keyword(s):  
Nuclear Import ◽  
Effective Concentration ◽  
Effective Vaccine ◽  
Mechanistic Analysis ◽  
Viral Cdna ◽  
Anti Hiv ◽  
Hiv 1 ◽  
Rapid Emergence ◽  
Infection Experiments

ABSTRACTIn the absence of an effective vaccine against HIV-1 infection, anti-HIV-1 strategies play a major role in disease control. However, the rapid emergence of drug resistance against all currently used anti-HIV-1 molecules necessitates the development of new antiviral molecules and/or strategies against HIV-1 infection. In this study, we have identified a benzamide derivative named AH0109 that exhibits potent anti-HIV-1 activity at an 50% effective concentration of 0.7 μM in HIV-1-susceptible CD4+C8166 T cells. Mechanistic analysis revealed that AH0109 significantly inhibits both HIV-1 reverse transcription and viral cDNA nuclear import. Furthermore, our infection experiments indicated that AH0109 is capable of disrupting the replication of HIV-1 strains that are resistant to the routinely used anti-HIV-1 drugs zidovudine, lamivudine, nevirapine, and raltegravir. Together, these findings provide evidence for a newly identified antiviral molecule that can potentially be developed as an anti-HIV-1 agent.

scholarly journals HIV-1 resists MxB inhibition of viral Rev protein

2020 ◽  
Vol 9 (1) ◽  
pp. 2030-2045
Author(s):  
Zhen Wang ◽  
Keli Chai ◽  
Qian Liu ◽  
Dong-Rong Yi ◽  
Qinghua Pan ◽  
...  
Keyword(s):  
Hiv 1 ◽  
Rev Protein
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