Interaction of Eukaryotic Initiation Factor 5A with the Human Immunodeficiency Virus Type 1 Rev Response Element RNA and U6 snRNA Requires Deoxyhypusine or Hypusine Modification

Neurosignals ◽  
1997 ◽  
Vol 6 (3) ◽  
pp. 166-174 ◽  
Author(s):  
Yi Ping Liu ◽  
Martin Nemeroff ◽  
Yong Ping Yan ◽  
Kuang Yu Chen
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Response Element ◽  
Rev Response Element ◽  
U6 Snrna ◽  
Immunodeficiency Virus

scholarly journals Eukaryotic initiation factor 5A is a cellular target of the human immunodeficiency virus type 1 Rev activation domain mediating trans-activation.

1993 ◽  
Vol 123 (6) ◽  
pp. 1309-1320 ◽  
Author(s):  
M Ruhl ◽  
M Himmelspach ◽  
G M Bahr ◽  
F Hammerschmid ◽  
H Jaksche ◽  
...  
Keyword(s):  
Gene Expression ◽  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Activation Domain ◽  
Immunodeficiency Virus ◽  
Hiv 1

Expression of human immunodeficiency virus type 1 (HIV-1) structural proteins requires the presence of the viral trans-activator protein Rev. Rev is localized in the nucleus and binds specifically to the Rev response element (RRE) sequence in viral RNA. Furthermore, the interaction of the Rev activation domain with a cellular cofactor is essential for Rev function in vivo. Using cross-linking experiments and Biospecific Interaction Analysis (BIA) we identify eukaryotic initiation factor 5A (eIF-5A) as a cellular factor binding specifically to the HIV-1 Rev activation domain. Indirect immunofluorescence studies demonstrate that a significant fraction of eIF-5A localizes to the nucleus. We also provide evidence that Rev transactivation is functionally mediated by eIF-5A in Xenopus oocytes. Furthermore, we are able to block Rev function in mammalian cells by antisense inhibition of eIF-5A gene expression. Thus, regulation of HIV-1 gene expression by Rev involves the targeting of RRE-containing RNA to components of the cellular translation initiation complex.

Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element

1991 ◽  
Vol 11 (5) ◽  
pp. 2567-2575
Author(s):  
C Fankhauser ◽  
E Izaurralde ◽  
Y Adachi ◽  
P Wingfield ◽  
U K Laemmli
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Nucleolar Protein ◽  
Response Element ◽  
Rev Response Element ◽  
Cell Extracts ◽  
Immunodeficiency Virus ◽  
Protein B23

The human immunodeficiency virus type 1 (HIV) Rev protein is thought to be involved in the export of unspliced or singly spliced viral mRNAs from the nucleus to the cytoplasm. This function is mediated by a sequence-specific interaction with a cis-acting RNA element, the Rev response element (RRE), present in these intron-containing RNAs. To identify possible host proteins involved in Rev function, we fractionated nuclear cell extracts with a Rev affinity column. A single, tightly associated Rev-binding protein was identified; this protein is the mammalian nucleolar protein B23. The interaction between HIV Rev and B23 is very specific, as it was observed in complex cell extracts. The complex is also very stable toward dissociation by high salt concentrations. Despite the stability of the Rev-B23 protein complex, the addition of RRE, but not control RNA, led to the displacement of B23 and the formation of a specific Rev-RRE complex. The mammalian nucleolar protein B23 or its amphibian counterpart No38 is believed to function as a shuttle receptor for the nuclear import of ribosomal proteins. B23 may also serve as a shuttle for the import of HIV Rev from the cytoplasm into the nucleus or nucleolus to allow further rounds of export of RRE-containing viral RNAs.

scholarly journals Rev regulates translation of human immunodeficiency virus type 1 RNAs

2009 ◽  
Vol 90 (5) ◽  
pp. 1141-1147 ◽  
Author(s):  
Harriet C. T. Groom ◽  
Emma C. Anderson ◽  
John A. Dangerfield ◽  
Andrew M. L. Lever
Keyword(s):  
Human Immunodeficiency Virus ◽  
Binding Site ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Untranslated Region ◽  
Response Element ◽  
Rev Response Element ◽  
Immunodeficiency Virus ◽  
Hiv 1

Full-length human immunodeficiency virus type 1 (HIV-1) RNA acts as both mRNA, encoding Gag and Gag–Pol polyproteins, and genomic RNA. Translation of this RNA must be tightly controlled to allow sufficient protein synthesis prior to a switch to particle production. The viral protein Rev stimulates nuclear export of unspliced HIV-1 RNAs containing the Rev response element, but may also stimulate translation of these RNAs. We previously identified an additional Rev binding site in the 5′ untranslated region of the HIV-1 RNA. We show that Rev inhibits translation non-specifically at high concentrations and stimulates translation of HIV-1 RNAs at intermediate concentrations in vitro. Stimulation is dependent on the presence of the Rev binding site within the 5′ untranslated region and not on the Rev response element. In COS-1 cells, translation from an HIV-1 reporter is specifically increased by coexpression of Rev.

scholarly journals Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element.

1991 ◽  
Vol 11 (5) ◽  
pp. 2567-2575 ◽  
Author(s):  
C Fankhauser ◽  
E Izaurralde ◽  
Y Adachi ◽  
P Wingfield ◽  
U K Laemmli
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Nucleolar Protein ◽  
Response Element ◽  
Rev Response Element ◽  
Cell Extracts ◽  
Immunodeficiency Virus ◽  
Protein B23

The human immunodeficiency virus type 1 (HIV) Rev protein is thought to be involved in the export of unspliced or singly spliced viral mRNAs from the nucleus to the cytoplasm. This function is mediated by a sequence-specific interaction with a cis-acting RNA element, the Rev response element (RRE), present in these intron-containing RNAs. To identify possible host proteins involved in Rev function, we fractionated nuclear cell extracts with a Rev affinity column. A single, tightly associated Rev-binding protein was identified; this protein is the mammalian nucleolar protein B23. The interaction between HIV Rev and B23 is very specific, as it was observed in complex cell extracts. The complex is also very stable toward dissociation by high salt concentrations. Despite the stability of the Rev-B23 protein complex, the addition of RRE, but not control RNA, led to the displacement of B23 and the formation of a specific Rev-RRE complex. The mammalian nucleolar protein B23 or its amphibian counterpart No38 is believed to function as a shuttle receptor for the nuclear import of ribosomal proteins. B23 may also serve as a shuttle for the import of HIV Rev from the cytoplasm into the nucleus or nucleolus to allow further rounds of export of RRE-containing viral RNAs.

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