Sequence requirements for nucleolar localization of human T cell leukemia virus type I pX protein, which regulates viral RNA processing

Siomi, Haruhiko; Shida, Hisatoshi; Nam, Sung Min; Nosaka, Tetsuya; Maki, Masatoshi; Hatanaka, Masakazu

doi:10.1016/0092-8674(88)90043-8

Cited by 294 publications

(207 citation statements)

References 31 publications

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“…The cDNA of the fully spliced transcript of HTLV-1 mRNA was subcloned into pcDNA1 to form pcDNA-RexLTR. The viral eDNA was subcloned as a HindIII fragment pKCR27x [10]. pcDNA-Rex contained the first half, a HindIII-SmaI fragment, of the viral eDNA used in pcDNA-RexLTR, pcDNA-LTR carries the 3' half, the SmaI-HindIII fragment, of the viral eDNA used.…”

Section: Expression Plasmidsmentioning

confidence: 99%

“…We were interested to establish whether Rex binds to the RexRE of cognate RNAs in nucleoli in view of the strong nucleolar localisation signal present on Rex protein [10]. We chose to locate viral RNAs expressed from segments of HTLV-1 in COS cells using the high resolution of fluorescence in situ hybridisation.…”

Section: Assessment Of Intracellular Distribution Of Mrna By Fishmentioning

confidence: 99%

“…Despite ~heir lack of sequence homology both proteins contain two orresponding functional domains. The N-terminal domain is ~ich in basic amino acid residues and serves as a nuclear i ocalisation signal, which also has nucleolar localising capabilty [10]. In addition the same domain is the site for multi-' Corresponding author.…”

Section: ! Introductionmentioning

confidence: 99%

“…The nucleolar localisation signal (NOS) of Rex is contained in the N-terminal 20 aa and can direct nucleolar localisation of chimeras of proteins normally expressed in the cytosol [10]. A functional NOS in Rex has been shown to be critical for Rex activitypoint mutations which abrogate the nucleolar localising capacity of the protein also inhibit completely the ability of Rex to promote transport of unspliced forms of viral RNA out of the nucleus [24].…”

Section: ! Introductionmentioning

confidence: 99%

“…Mutation of the NOS can abrogate both RNA binding and nucleolar localisation and it is not clear from these data whether a lack of Rex in the nucleoli is part of the reason for the loss of the functioning of Rex in vivo. Although Rex is heavily expressed in nucleoli staining in the nucleoplasm is also evident [10] and detailed immunohistochemical analysis of Rev localisation reveals a variety of staining patterns in the nucleolus, nucleoplasm and cytoplasm [27]. Chimeras of Rev activation domain and transcription factor DNA binding domains indicate that the effector domain of Rev can work outside nucleoli in the nucleoplasm [28].…”

Section: ! Introductionmentioning

confidence: 99%

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Enhancement of nucleocytoplasmic export of HTLV‐1 Rex mRNA through cis and trans interactions of the mRNA with the complex of Rex protein and Rex‐responsive element

White

1996

FEBS Letters

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p27 rex of HTLV-1 promotes nucleocytoplasmic t xport of viral mRNAs through binding of the Rex-response element (RexRE) present at the 3' end of the viral transcripts in ds with respect to the ORFs of the viral mRNAs. We have found that expression of the RexRE in trans, as a separate RNA, still allows Rex protein to promote export of viral mRNAs lacking the RexRE. The data suggest the formation of a ternary complex between Rex protein, RexRE and upstream elements of viral mRNA and hence the existence of secondary sites of interaction between Rex protein and viral RNAs.~ey words: mRNA export; HTLV-1; Retrovirus; p27rex; t,'~ex-responsive element; Fluorescence in situ hybridisation !. IntroductionHuman T-cell leukaemic virus type 1 (HTLV-1) is a retro-, irus trophic for CD4 + T-cells associated with an aggressive lorm of leukaemia, adult T-cell leukaemia [1,2], and with a ~eurological disorder, tropical spastic paraparesis, also due to infection of T-cells [3]. In order to co-ordinate the regulation ,,f the structural and viral proteins necessary for viral replication a nuclear protein, Rex, encoded in the viral genome, makes efficient use of variably spliced reading frames in the , iral genome (reviewed in [4]). In the presence of Rex incom-1,1etely spliced transcripts of viral RNA are expressed in the • ytoplasm, allowing expression of proteins from the unspliced :ag-pol transcript and the singly spliced env transcript. In the ,,bsence of Rex the incompletely spliced transcripts remain .equestered in the nucleus to be degraded or for completion ,,f splicing [5,6]. Completely spliced transcripts encode the ~egulatory proteins of the virus, Tax and Rex [5]. Rex works i~y binding directly to a highly structured element of RNA of ~kbout 250 bases present in the viral transcripts, the Rex-re-, ponsive element (RexRE) [7][8][9]. Details of the mechanism of ~tction of Rex, and its analogue Rev from human immunode-!tciency virus (HIV) type 1, are becoming apparent. Despite ~heir lack of sequence homology both proteins contain two orresponding functional domains. The N-terminal domain is ~ich in basic amino acid residues and serves as a nuclear i ocalisation signal, which also has nucleolar localising capabilty [10]. In addition the same domain is the site for multi-' Corresponding author. Fax: (44) (171) 955-4191. E-mail: k.white@umds.ac.ukIbbreviations. FITC, fluorescein isothiocyanate; HIV, human immunodeficiency virus; HTLV-1, human T-cell leukaemic virus type 1 ; NOS, nucleolar localisation signal; RexRE, Rex-responsive element merisation [11] and for binding to the responsive element on the viral RNA [8,12]. A C-terminal domain encodes a leucinerich effector domain which includes a recently characterised nuclear export signal [13,14]. The combination of nuclear import and export signals accounts for the demonstrated ability of Rev to shuttle between the nucleus and cytoplasm [15,16].Two models have been proposed to account for the retention of unspliced viral mRNAs in the nucleus and for the relief of the ...

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Section: Expression Plasmidsmentioning

confidence: 99%

Section: Assessment Of Intracellular Distribution Of Mrna By Fishmentioning

confidence: 99%

Section: ! Introductionmentioning

confidence: 99%

Section: ! Introductionmentioning

confidence: 99%

Section: ! Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Enhancement of nucleocytoplasmic export of HTLV‐1 Rex mRNA through cis and trans interactions of the mRNA with the complex of Rex protein and Rex‐responsive element

White

1996

FEBS Letters

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Nucleolar targeting of 5S RNA inXenopus laevis oocytes: Somatic-type nucleotide substitutions enhance nucleolar localization

North¹,

Allison²

1998

J. Cell. Biochem.

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In Xenopus laevis oocytes, 5S RNA is stored in the cytoplasm until vitellogenesis, at which time it is imported into the nucleus and targeted to nucleoli for ribosome assembly. This article shows that throughout oogenesis there is a pool of nuclear 5S RNA which is not nucleolar-associated. This distribution reflects that of oocyte-type 5S RNA, which is the major 5S RNA species in oocytes; only small amounts of somatic-type, which differs by six nucleotides, are synthesized. Indeed, 32P-labeled oocyte-type 5S RNA showed a degree of nucleolar localization similar to endogenous 5S RNA (33%) after microinjection. In contrast, 32P-labeled somatic-type 5S RNA showed significantly enhanced localization, whereby 70% of nuclear RNA was associated with nucleoli. A chimeric RNA molecule containing only one somatic-specific nucleotide substitution also showed enhanced localization, in addition to other somatic-specific phenotypes, including enhanced nuclear import and ribosome incorporation. The distribution of 35S-labeled ribosomal protein L5 was similar to that of oocyte-type 5S RNA, even when preassembled with somatic-type 5S RNA. The distribution of a series of 5S RNA mutants was also analyzed. These mutants showed various degrees of localization, suggesting that the efficiency of nucleolar targeting can be influenced by many discrete regions of the 5S RNA molecule.

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Dual cytoplasmic and nuclear distribution of the novel arsenite‐stimulated human ATPase (hASNA‐I)

Kurdi-Haidar

Hom

Flittner

et al. 1998

J of Cellular Biochemistry

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The arsenite-stimulated human ATPase (hASNA-I) protein is a distinct human ATPase whose cDNA was cloned by sequence homology to the Escherichia coli ATPase arsA. Its subcellular localization in human malignant melanoma T289 cells was examined to gain insight into the role of hASNA-I in the physiology of human cells. Immunocytochemical staining using the specific anti-hASNA-I monoclonal antibody 5G8 showed a cytoplasmic, perinuclear, and nucleolar distribution. Subcellular fractionation indicated that the cytoplasmic hASNA-I was soluble and that the perinuclear distribution was due to association with the nuclear membrane rather than with the endoplasmic reticulum. Its presence in the nucleolus was confirmed by showing colocalization with an antibody of known nucleolar specificity. Further immunocytochemical analysis showed that the hASNA-I at the nuclear membrane was associated with invaginations into the nucleus in interphase cells. These results indicate that hASNA-I is a paralogue of the bacterial ArsA protein and suggest that it plays a role in the nucleocytoplasmic transport of a nucleolar component.

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Sequence requirements for nucleolar localization of human T cell leukemia virus type I pX protein, which regulates viral RNA processing

Cited by 294 publications

References 31 publications

Enhancement of nucleocytoplasmic export of HTLV‐1 Rex mRNA through cis and trans interactions of the mRNA with the complex of Rex protein and Rex‐responsive element

Enhancement of nucleocytoplasmic export of HTLV‐1 Rex mRNA through cis and trans interactions of the mRNA with the complex of Rex protein and Rex‐responsive element

Nucleolar targeting of 5S RNA inXenopus laevis oocytes: Somatic-type nucleotide substitutions enhance nucleolar localization

Dual cytoplasmic and nuclear distribution of the novel arsenite‐stimulated human ATPase (hASNA‐I)

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