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Comparative Study | Journal Article | Research Support, Non-U.S. Gov't

Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay.

H P Bogerd, R A Fridell, R E Benson, J Hua, B R Cullen
H P Bogerd
Howard Hughes Medical Institute and Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.
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R A Fridell
Howard Hughes Medical Institute and Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.
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R E Benson
Howard Hughes Medical Institute and Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.
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J Hua
Howard Hughes Medical Institute and Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.
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B R Cullen
Howard Hughes Medical Institute and Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.
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DOI: 10.1128/MCB.16.8.4207
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ABSTRACT

The Rex protein of human T-cell leukemia virus type 1, like the functionally equivalent Rev protein of human immunodeficiency virus type 1, contains a leucine-rich activation domain that specifically interacts with the human nucleoporin-like Rab/hRIP cofactor. Here, this Rex sequence is shown to function also as a protein nuclear export signal (NES). Rex sequence libraries containing randomized forms of the activation domain/NES were screened for retention of the ability to bind Rab/hRIP by using the yeast two-hybrid assay. While the selected sequences differed widely in primary sequence, all were functional as Rex activation domains. In contrast, randomized sequences that failed to bind Rab/hRIP lacked Rex activity. The selected sequences included one with homology to the Rev activation domain/NES and a second that was similar to the NES found in the cellular protein kinase inhibitor alpha. A highly variant, yet fully active, activation domain sequence selected on the basis of Rab/hRIP binding retained full NES function even though this sequence preserved only a single leucine residue. In contrast, nonfunctional activation domain mutants that were unable to bind Rab/hRIP had also lost NES function. These data demonstrate that NES activity is a defining characteristic of the activation domains found in the Rev/Rex class of retroviral regulatory proteins and strongly support the hypothesis that the Rab/hRIP cofactor plays a critical role in mediating the biological activity of these NESs. In addition, these data suggest a consensus sequence for NESs of the Rev/Rex class.

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Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay.
H P Bogerd, R A Fridell, R E Benson, J Hua, B R Cullen
Molecular and Cellular Biology Aug 1996, 16 (8) 4207-4214; DOI: 10.1128/MCB.16.8.4207

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Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay.
H P Bogerd, R A Fridell, R E Benson, J Hua, B R Cullen
Molecular and Cellular Biology Aug 1996, 16 (8) 4207-4214; DOI: 10.1128/MCB.16.8.4207
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