Importance of mammalian nuclear-envelope nucleoside triphosphatase in nucleo-cytoplasmic transport of ribonucleoproteins

Agutter, Paul S.; McCaldin, B; McArdle, Harry J

doi:10.1042/bj1820811

Cited by 99 publications

(58 citation statements)

References 34 publications

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“…Investigations in my laboratory (Agutter et al, 1976(Agutter et al, , 1979b and by others (Clawson & Clawson et al, 1978) supported the fourth of these interpretations. More specifically, Agutter et al (1976, 1979b) have provided evidence that ATP hydrolysis occurs at an NTPase located in the nuclear-pore complex (Yasuzumi & Tsubo, 1966;Yasuzumi et al, 1967;Chardonnet & Dales, 1972;Franke, 1974), and that this event is necessary for RNA transport.…”

supporting

confidence: 62%

“…More specifically, Agutter et al (1976, 1979b) have provided evidence that ATP hydrolysis occurs at an NTPase located in the nuclear-pore complex (Yasuzumi & Tsubo, 1966;Yasuzumi et al, 1967;Chardonnet & Dales, 1972;Franke, 1974), and that this event is necessary for RNA transport. However, the findings of Agutter et al (1979b) and Clawson et al (1978) are not wholly consistent with one another. The main differences are that: (a) Clawson et al (1978) reported that ADP stimulated RNA release to a significant extent, but Agutter et al (1979b) were unable to repeat this observation; (b) Clawson et al (1978) found that pchloromercuribenzoate markedly stimulated RNA release in the presence of ATP, whereas Agutter et a!.…”

mentioning

confidence: 43%

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Influence of nucleotides, cations and nucleoside triphosphatase inhibitors on the release of ribonucleic acid from isolated rat liver nuclei

Agutter¹

1980

Biochemical Journal

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The reasons underlying reported discrepancies in the effects of ATP, ADP, adenosine 5'-[Ify-methyleneltriphosphate, AMP + PP1, p-chloromercuribenzoate and F-on RNA efflux from isolated rat liver nuclei and on nuclear-envelope nucleoside triphosphatase activity were investigated. The stimulatory effect of ADP was attributed to myokinase activity associated with the nuclei; this activity was eluted on repeated washing with nuclear incubation medium. In the absence of Ca2+ and Mn2+, ATP, adenosine 5'-[Iymethyleneltriphosphate and AMP+ PP1 were found to promote release of both DNA and RNA. In the presence of 0.5 mM-Ca2+ and 0.3 mM-Mn2 , only ATP promoted RNA efflux to a significant extent. In the absence of spermidine, Ca2+ and Mn2+, nuclei released large quantities of DNA and RNA into the medium; this effect was promoted by p-chloromercuribenzoate. In the presence of the three cations, however, pchloromercuribenzoate inhibited RNA efflux. F-caused a slight leakage of DNA from nuclei. The results are discussed in terms of models for the effects of ATP and analogues on RNA efflux and nuclear stability.The stimulation of RNA release from isolated nuclei by ATP and related compounds has been investigated in several laboratories and the effect has been interpreted in at least four different ways.(1) The ATP chelates bivalent metal ions in the medium, promoting release of heterogeneous nuclear RNA-protein complexes from the chromatin (Ishi-

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supporting

confidence: 62%

mentioning

confidence: 43%

Influence of nucleotides, cations and nucleoside triphosphatase inhibitors on the release of ribonucleic acid from isolated rat liver nuclei

Agutter¹

1980

Biochemical Journal

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“…The release of mRNA, unlike that of ribosomal RNA, is dependent on ATP hydrolysis. This is compatible with the requirement for polyadenylation in the processing of mRNA precursors [45] as well as the involvement of nuclear-porecomplex triphosphatase in the transport of mRNA as proposed by Clawson et al [46] and Agutter et al [47]. That RNA transport still occurs after treatment of nuclei with non-ionic detergent confirms the findings of Roy et al…”

Section: Discussionsupporting

confidence: 80%

“…[13], and suggests that nuclear membrane phospholipid is not rcquired, contrary to the conclusions of others [47,48]. The molecular hybridisation assays show that the transported poly(A)-rich R N A is a diverse mixture of RNA sequences which is similar to that expected for a population of newly transported mRNAs.…”

Section: Discussioncontrasting

confidence: 48%

Isolation and Purification of Rat Hepatoma Nuclei Active in the Transport of Messenger RNA in vitro

Jacobs

Birnie

1982

Eur J Biochem

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1. A variety of procedures for obtaining metabolically active nuclei from rat hepatoma tissue-culture (HTC) cells has been explored. All gave preparations which were, to a greater or lesser extent, contaminated with cytoplasmic RNA, which appeared to be absorbed non-specifically during the lysis of the cells.2. A medium containing spermidine, monovalent and divalent cations, and cytosol has bccn defined in which the integrity of the isolated nuclei was maintained during incubation in virro.3. The release of steady-state-labelled and pulse-labelled RNA from HTC cell nuclei during incubation in this medium has been studied. The transport of both was dependent on ATP and cytosol, but was distinguishable by the kinetics and by the fact that only the transport of pulse-labelled RNA appeared to involve hydrolysis of ATP. Transported RNA included ribosomal R N A and messenger-likc RNA as judged by criteria of size, oligo(dT)-cellulose binding, and organisation into ribonucleoproteins. A large proportion of the cytoplasmic R N A which adhered to the nuclei was also released during incubation in v i m .4. Although the poly(A)-rich RNA transported in v i m was contaminated with poly(A)-rich RNA sequences arising from non-specific leakage of nuclear RNA and from the release of nucleus-adherent cytoplasmic RNA, the extent of this contamination was comparatively small (10"; and 10-15% by weight respcctively). Thc transportcd poly(A)-rich RNA has been shown to consist of a complex mixture of sequences at heterogeneous abundanccs, resembling polysomal poly(A)-rich mRNA from HTC cells.5. The pattern of relative abundanccs of the sequences in transported poly(A)-rich RNA was intermediate betwieen that of polysomal and nuclear poly(A)-rich RNAs, and indicated that some degree of sequence-spccific selection of processing, or transport, or both, can be maintained in isolated nuclei. Sequence-specific selcction in vitro at the level of individual poly(A)-rich RNA sequences was detected using cloned cDNAs for poly(A)-rich polysomal RNA sequences.

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“…In contrast to the nonhistone, actin or P-tubulin mRNA, all three histone mRNA studied (H4, H2B and H1) were released into the postnuclear supernatant also in the absence of nucleotides, although at lower rates (about 50% of that in the presence of ATP). Addition of inhibitors of the nuclear envelope NTPase, previously found to inhibit transport of poly(A)-rich mRNA [46], caused only a slight decrease in efflux of histone mRNA. A striking argument for an involvement of the NTPase in mRNA transport was the finding that ATP hydrolysis by this enzyme and RNA efflux display similar activation energies [48].…”

Section: Discussionmentioning

confidence: 99%

Energy requirement and kineties of transport of poly(A)‐free histone mRNA compared to poly(A)‐rich mRNA from isolated L‐cell nuclei

Schröder

Friese

Bachmann

et al. 1989

European Journal of Biochemistry

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ATP-promoted efflux of poly(A)-rich RNA from isolated nuclei of prelabeled mouse lymphoma L5178y cells has an activation energy of 51.5 kJ/mol, similar to that found for the nuclear envelope nucleoside triphosphatase (48.1 kJ/mol) assumed to be involved in mediating nucleocytoplasmic transport of at least some RNA. Here we show that efflux of two specific poly(A)-rich mRNAs (actin and P-tubulin) from isolated L-cell nuclei is almost totally dependent on the presence of ATP, while efflux of poly(A)-free histone mRNA (H4, H2B, and H1) also occurs to a marked extent in the absence of this nucleotide. Measurements of temperature dependence of transport rate revealed an activation energy of 56.1 kJ/mol for actin mRNA, while the activation energy for histone-H4-mRNA efflux was in the same range as that found for ATP-induced release of RNA from demembranated nuclei (about 15-20 kJ/mol). Addition of nonhydrolyzable nucleotide analogs of ATP to the in vitro system used for measurement of RNA transport did not result in release of nonhistone mRNA (actin), but enhanced the efflux of H4 mRNA to approximately the same extent as ATP. Although not absolutely required, addition of ATP stimulated the rate of export of histone mRNA about twofold. Only the poly(A)-rich RNA, but not the poly(A)-free RNA, released from isolated nuclei was found to compete with poly(A) for the nuclear envelope mRNAbinding site, indicating the mechanism of transport for both RNA classes to be distinct. Export of both nonhistone and histone mRNA was found to be inhibited by a monoclonal antibody against a p60 nuclear-pore-complex antigen. This antibody had no effect on the nucleoside triphosphatase, mediating transport of poly(A)-rich mRNA.

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Importance of mammalian nuclear-envelope nucleoside triphosphatase in nucleo-cytoplasmic transport of ribonucleoproteins

Cited by 99 publications

References 34 publications

Influence of nucleotides, cations and nucleoside triphosphatase inhibitors on the release of ribonucleic acid from isolated rat liver nuclei

Influence of nucleotides, cations and nucleoside triphosphatase inhibitors on the release of ribonucleic acid from isolated rat liver nuclei

Isolation and Purification of Rat Hepatoma Nuclei Active in the Transport of Messenger RNA in vitro

Energy requirement and kineties of transport of poly(A)‐free histone mRNA compared to poly(A)‐rich mRNA from isolated L‐cell nuclei

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