ArticleJournal of virology1992
Dominant-negative mutants are clustered in a domain of the human T-cell leukemia virus type I Rex protein: implications for trans dominance.
Article in Journal of virology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Human Retrovirus Genomic RNA Packaging.Viruses · 2022Review
- Is unphosphorylated Rex, as multifunctional protein of HTLV-1, a fully intrinsically disordered protein? An in silico study.Biochemistry and biophysics reports · 2016Article
- Role of Nucleocytoplasmic RNA Transport during the Life Cycle of Retroviruses.Frontiers in microbiology · 2012Article
- Human T-cell leukemia virus type 2 Rex carboxy terminus is an inhibitory/stability domain that regulates Rex functional activity and viral replication.Journal of virology · 2009Article
- Review
- Mutational analysis of bovine leukemia virus Rex: identification of a dominant-negative inhibitor.Journal of virology · 2005Article
- The human T-cell leukemia virus Rex protein.Frontiers in bioscience : a journal and virtual library · 2005Review
- Functional domain structure of human T-cell leukemia virus type 2 rex.Journal of virology · 2003Article
- Article
- A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of human T-cell leukemia virus type 1 Rex protein.Molecular and cellular biology · 2003Article
- Rat CRM1 is responsible for the poor activity of human T-cell leukemia virus type 1 Rex protein in rat cells.Journal of virology · 2001Article
- Phosphorylation of two serine residues regulates human T-cell leukemia virus type 2 Rex function.Journal of virology · 2001Article
- Titration of cellular export factors, but not heteromultimerization, is the molecular mechanism of trans-dominant HTLV-1 rex mutants.Oncogene · 1999Article
- Multimer formation is not essential for nuclear export of human T-cell leukemia virus type 1 Rex trans-activator protein.Journal of virology · 1998Article
- Involvement of human CRM1 (exportin 1) in the export and multimerization of the Rex protein of human T-cell leukemia virus type 1.Journal of virology · 1998Article
- The human T-cell lymphotropic virus type 1 Tof protein contains a bipartite nuclear localization signal that is able to functionally replace the amino-terminal domain of Rex.Journal of virology · 1997Article
- Effects of translation initiation factor eIF-5A on the functioning of human T-cell leukemia virus type I Rex and human immunodeficiency virus Rev inhibited trans dominantly by a Rex mutant deficient in RNA binding.Journal of virology · 1995Article
- Complete nucleotide sequence of an Amerindian human T-cell lymphotropic virus type II (HTLV-II) isolate: identification of a variant HTLV-II subtype b from a Guaymi Indian.Journal of virology · 1993Article
- Dominant negative mutants of human T-cell leukemia virus type I Rex and human immunodeficiency virus type 1 Rev fail to multimerize in vivo.Journal of virology · 1993Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 27-kDa Rex trans-acting protein appears to be essential for replication of human T-cell leukemia virus type I. Mutations introduced outside of the Rex RNA-binding domain-nucleolar localization signal display either wild-type activity or, conversely, yield dominant-negative proteins. We generated missense mutations in a particular domain of the Rex protein (amino acid residues 54 to 69) which is characterized by a cluster of dominant-negative mutants. Our results indicate that amino acids 57 to 67 are critically important for Rex function mediated through the RxRE cis-acting RNA sequence. Within this domain, only amino acids 61 to 63 could be mutated without loss of function. All other missense and deletion mutants yielded dominant-negative proteins. In vitro RNA-binding studies performed with glutathione S-transferase-Rex fusion proteins demonstrated that all of the mutant Rex proteins interacted specifically with RxRE RNA. Analysis of chimeric Rex-Rev proteins suggests that this Rex domain is important for oligomerization.
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