Thermal diminution and augmentation of the retention of transportable rRNA in nuclear envelope-free nuclei
We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitati...
Ausführliche Beschreibung
Gespeichert in:
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1984 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression - Amsterdam : Elsevier, 782(1984), 2, Seite 187-194 |
| Übergeordnetes Werk: |
volume:782 ; year:1984 ; number:2 ; pages:187-194 |
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| 520 | |a We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitatively the same in terms of rRNA pattern, sedimentation coefficients and buoyant densities. At 8^oC, however, significantly fewer ribosomal ribonucleoprotein particles can be maximally exported than at 28^oC, though nuclei contain enough potentially transportable particles. These are increasingly released with increasing temperatures. Under conditions non-permissive for export, temperature elevation decreases the number of the potentially transportable ribosomal ribonucleoprotein particles in nuclei. Our data show: (i) transportable ribosomal ribonucleoprotein particles inside nuclei are not 'free', but rather are subject to a complex temperature-sensitive retention: this retention is gradually diminished under export conditions and augmented under non-permissive export conditions with increasing temperatures. (ii) These retention mechanisms operate at an intranuclear level preceding the ribosomal ribonucleoprotein passage through the nuclear envelope pore complexes, i.e., the nuclear envelope regulates neither the number of potentially transportable ribosomal ribonucleoprotein particles in nuclei nor the number of those particles which can be maximally exported from nuclei at a given temperature. We suggest that these retention mechanisms involve temperature-sensitive domains of the nuclear matrix. | ||
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(DE-627)NLEJ186807406 (DE-599)GBVNLZ186807406 DE-627 ger DE-627 rakwb eng Thermal diminution and augmentation of the retention of transportable rRNA in nuclear envelope-free nuclei 1984 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitatively the same in terms of rRNA pattern, sedimentation coefficients and buoyant densities. At 8^oC, however, significantly fewer ribosomal ribonucleoprotein particles can be maximally exported than at 28^oC, though nuclei contain enough potentially transportable particles. These are increasingly released with increasing temperatures. Under conditions non-permissive for export, temperature elevation decreases the number of the potentially transportable ribosomal ribonucleoprotein particles in nuclei. Our data show: (i) transportable ribosomal ribonucleoprotein particles inside nuclei are not 'free', but rather are subject to a complex temperature-sensitive retention: this retention is gradually diminished under export conditions and augmented under non-permissive export conditions with increasing temperatures. (ii) These retention mechanisms operate at an intranuclear level preceding the ribosomal ribonucleoprotein passage through the nuclear envelope pore complexes, i.e., the nuclear envelope regulates neither the number of potentially transportable ribosomal ribonucleoprotein particles in nuclei nor the number of those particles which can be maximally exported from nuclei at a given temperature. We suggest that these retention mechanisms involve temperature-sensitive domains of the nuclear matrix. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Wunderlich, F. oth Giese, G. oth Speth, V. oth in Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression Amsterdam : Elsevier 782(1984), 2, Seite 187-194 (DE-627)NLEJ176932224 (DE-600)2209522-6 0167-4781 nnns volume:782 year:1984 number:2 pages:187-194 http://linkinghub.elsevier.com/retrieve/pii/0167-4781(84)90023-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 782 1984 2 187-194 |
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(DE-627)NLEJ186807406 (DE-599)GBVNLZ186807406 DE-627 ger DE-627 rakwb eng Thermal diminution and augmentation of the retention of transportable rRNA in nuclear envelope-free nuclei 1984 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitatively the same in terms of rRNA pattern, sedimentation coefficients and buoyant densities. At 8^oC, however, significantly fewer ribosomal ribonucleoprotein particles can be maximally exported than at 28^oC, though nuclei contain enough potentially transportable particles. These are increasingly released with increasing temperatures. Under conditions non-permissive for export, temperature elevation decreases the number of the potentially transportable ribosomal ribonucleoprotein particles in nuclei. Our data show: (i) transportable ribosomal ribonucleoprotein particles inside nuclei are not 'free', but rather are subject to a complex temperature-sensitive retention: this retention is gradually diminished under export conditions and augmented under non-permissive export conditions with increasing temperatures. (ii) These retention mechanisms operate at an intranuclear level preceding the ribosomal ribonucleoprotein passage through the nuclear envelope pore complexes, i.e., the nuclear envelope regulates neither the number of potentially transportable ribosomal ribonucleoprotein particles in nuclei nor the number of those particles which can be maximally exported from nuclei at a given temperature. We suggest that these retention mechanisms involve temperature-sensitive domains of the nuclear matrix. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Wunderlich, F. oth Giese, G. oth Speth, V. oth in Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression Amsterdam : Elsevier 782(1984), 2, Seite 187-194 (DE-627)NLEJ176932224 (DE-600)2209522-6 0167-4781 nnns volume:782 year:1984 number:2 pages:187-194 http://linkinghub.elsevier.com/retrieve/pii/0167-4781(84)90023-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 782 1984 2 187-194 |
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(DE-627)NLEJ186807406 (DE-599)GBVNLZ186807406 DE-627 ger DE-627 rakwb eng Thermal diminution and augmentation of the retention of transportable rRNA in nuclear envelope-free nuclei 1984 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitatively the same in terms of rRNA pattern, sedimentation coefficients and buoyant densities. At 8^oC, however, significantly fewer ribosomal ribonucleoprotein particles can be maximally exported than at 28^oC, though nuclei contain enough potentially transportable particles. These are increasingly released with increasing temperatures. Under conditions non-permissive for export, temperature elevation decreases the number of the potentially transportable ribosomal ribonucleoprotein particles in nuclei. Our data show: (i) transportable ribosomal ribonucleoprotein particles inside nuclei are not 'free', but rather are subject to a complex temperature-sensitive retention: this retention is gradually diminished under export conditions and augmented under non-permissive export conditions with increasing temperatures. (ii) These retention mechanisms operate at an intranuclear level preceding the ribosomal ribonucleoprotein passage through the nuclear envelope pore complexes, i.e., the nuclear envelope regulates neither the number of potentially transportable ribosomal ribonucleoprotein particles in nuclei nor the number of those particles which can be maximally exported from nuclei at a given temperature. We suggest that these retention mechanisms involve temperature-sensitive domains of the nuclear matrix. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Wunderlich, F. oth Giese, G. oth Speth, V. oth in Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression Amsterdam : Elsevier 782(1984), 2, Seite 187-194 (DE-627)NLEJ176932224 (DE-600)2209522-6 0167-4781 nnns volume:782 year:1984 number:2 pages:187-194 http://linkinghub.elsevier.com/retrieve/pii/0167-4781(84)90023-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 782 1984 2 187-194 |
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(DE-627)NLEJ186807406 (DE-599)GBVNLZ186807406 DE-627 ger DE-627 rakwb eng Thermal diminution and augmentation of the retention of transportable rRNA in nuclear envelope-free nuclei 1984 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitatively the same in terms of rRNA pattern, sedimentation coefficients and buoyant densities. At 8^oC, however, significantly fewer ribosomal ribonucleoprotein particles can be maximally exported than at 28^oC, though nuclei contain enough potentially transportable particles. These are increasingly released with increasing temperatures. Under conditions non-permissive for export, temperature elevation decreases the number of the potentially transportable ribosomal ribonucleoprotein particles in nuclei. Our data show: (i) transportable ribosomal ribonucleoprotein particles inside nuclei are not 'free', but rather are subject to a complex temperature-sensitive retention: this retention is gradually diminished under export conditions and augmented under non-permissive export conditions with increasing temperatures. (ii) These retention mechanisms operate at an intranuclear level preceding the ribosomal ribonucleoprotein passage through the nuclear envelope pore complexes, i.e., the nuclear envelope regulates neither the number of potentially transportable ribosomal ribonucleoprotein particles in nuclei nor the number of those particles which can be maximally exported from nuclei at a given temperature. We suggest that these retention mechanisms involve temperature-sensitive domains of the nuclear matrix. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Wunderlich, F. oth Giese, G. oth Speth, V. oth in Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression Amsterdam : Elsevier 782(1984), 2, Seite 187-194 (DE-627)NLEJ176932224 (DE-600)2209522-6 0167-4781 nnns volume:782 year:1984 number:2 pages:187-194 http://linkinghub.elsevier.com/retrieve/pii/0167-4781(84)90023-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 782 1984 2 187-194 |
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(DE-627)NLEJ186807406 (DE-599)GBVNLZ186807406 DE-627 ger DE-627 rakwb eng Thermal diminution and augmentation of the retention of transportable rRNA in nuclear envelope-free nuclei 1984 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitatively the same in terms of rRNA pattern, sedimentation coefficients and buoyant densities. At 8^oC, however, significantly fewer ribosomal ribonucleoprotein particles can be maximally exported than at 28^oC, though nuclei contain enough potentially transportable particles. These are increasingly released with increasing temperatures. Under conditions non-permissive for export, temperature elevation decreases the number of the potentially transportable ribosomal ribonucleoprotein particles in nuclei. Our data show: (i) transportable ribosomal ribonucleoprotein particles inside nuclei are not 'free', but rather are subject to a complex temperature-sensitive retention: this retention is gradually diminished under export conditions and augmented under non-permissive export conditions with increasing temperatures. (ii) These retention mechanisms operate at an intranuclear level preceding the ribosomal ribonucleoprotein passage through the nuclear envelope pore complexes, i.e., the nuclear envelope regulates neither the number of potentially transportable ribosomal ribonucleoprotein particles in nuclei nor the number of those particles which can be maximally exported from nuclei at a given temperature. We suggest that these retention mechanisms involve temperature-sensitive domains of the nuclear matrix. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Wunderlich, F. oth Giese, G. oth Speth, V. oth in Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression Amsterdam : Elsevier 782(1984), 2, Seite 187-194 (DE-627)NLEJ176932224 (DE-600)2209522-6 0167-4781 nnns volume:782 year:1984 number:2 pages:187-194 http://linkinghub.elsevier.com/retrieve/pii/0167-4781(84)90023-X GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 782 1984 2 187-194 |
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thermal diminution and augmentation of the retention of transportable rrna in nuclear envelope-free nuclei |
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Thermal diminution and augmentation of the retention of transportable rRNA in nuclear envelope-free nuclei |
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We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitatively the same in terms of rRNA pattern, sedimentation coefficients and buoyant densities. At 8^oC, however, significantly fewer ribosomal ribonucleoprotein particles can be maximally exported than at 28^oC, though nuclei contain enough potentially transportable particles. These are increasingly released with increasing temperatures. Under conditions non-permissive for export, temperature elevation decreases the number of the potentially transportable ribosomal ribonucleoprotein particles in nuclei. Our data show: (i) transportable ribosomal ribonucleoprotein particles inside nuclei are not 'free', but rather are subject to a complex temperature-sensitive retention: this retention is gradually diminished under export conditions and augmented under non-permissive export conditions with increasing temperatures. (ii) These retention mechanisms operate at an intranuclear level preceding the ribosomal ribonucleoprotein passage through the nuclear envelope pore complexes, i.e., the nuclear envelope regulates neither the number of potentially transportable ribosomal ribonucleoprotein particles in nuclei nor the number of those particles which can be maximally exported from nuclei at a given temperature. We suggest that these retention mechanisms involve temperature-sensitive domains of the nuclear matrix. |
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We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitatively the same in terms of rRNA pattern, sedimentation coefficients and buoyant densities. At 8^oC, however, significantly fewer ribosomal ribonucleoprotein particles can be maximally exported than at 28^oC, though nuclei contain enough potentially transportable particles. These are increasingly released with increasing temperatures. Under conditions non-permissive for export, temperature elevation decreases the number of the potentially transportable ribosomal ribonucleoprotein particles in nuclei. Our data show: (i) transportable ribosomal ribonucleoprotein particles inside nuclei are not 'free', but rather are subject to a complex temperature-sensitive retention: this retention is gradually diminished under export conditions and augmented under non-permissive export conditions with increasing temperatures. (ii) These retention mechanisms operate at an intranuclear level preceding the ribosomal ribonucleoprotein passage through the nuclear envelope pore complexes, i.e., the nuclear envelope regulates neither the number of potentially transportable ribosomal ribonucleoprotein particles in nuclei nor the number of those particles which can be maximally exported from nuclei at a given temperature. We suggest that these retention mechanisms involve temperature-sensitive domains of the nuclear matrix. |
| abstract_unstemmed |
We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitatively the same in terms of rRNA pattern, sedimentation coefficients and buoyant densities. At 8^oC, however, significantly fewer ribosomal ribonucleoprotein particles can be maximally exported than at 28^oC, though nuclei contain enough potentially transportable particles. These are increasingly released with increasing temperatures. Under conditions non-permissive for export, temperature elevation decreases the number of the potentially transportable ribosomal ribonucleoprotein particles in nuclei. Our data show: (i) transportable ribosomal ribonucleoprotein particles inside nuclei are not 'free', but rather are subject to a complex temperature-sensitive retention: this retention is gradually diminished under export conditions and augmented under non-permissive export conditions with increasing temperatures. (ii) These retention mechanisms operate at an intranuclear level preceding the ribosomal ribonucleoprotein passage through the nuclear envelope pore complexes, i.e., the nuclear envelope regulates neither the number of potentially transportable ribosomal ribonucleoprotein particles in nuclei nor the number of those particles which can be maximally exported from nuclei at a given temperature. We suggest that these retention mechanisms involve temperature-sensitive domains of the nuclear matrix. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ186807406</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707060632.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1984 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ186807406</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ186807406</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Thermal diminution and augmentation of the retention of transportable rRNA in nuclear envelope-free nuclei</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1984</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">We have examined the effect of temperature on the rRNA transport from nuclei isolated from Tetrahymena after removal of both nuclear membranes and pore complexes by 1% Triton X-100. These nuclei export rRNA as precursor ribosomal ribonucleoprotein particles at both 28^oC and 8^oC which are qualitatively the same in terms of rRNA pattern, sedimentation coefficients and buoyant densities. At 8^oC, however, significantly fewer ribosomal ribonucleoprotein particles can be maximally exported than at 28^oC, though nuclei contain enough potentially transportable particles. These are increasingly released with increasing temperatures. Under conditions non-permissive for export, temperature elevation decreases the number of the potentially transportable ribosomal ribonucleoprotein particles in nuclei. Our data show: (i) transportable ribosomal ribonucleoprotein particles inside nuclei are not 'free', but rather are subject to a complex temperature-sensitive retention: this retention is gradually diminished under export conditions and augmented under non-permissive export conditions with increasing temperatures. (ii) These retention mechanisms operate at an intranuclear level preceding the ribosomal ribonucleoprotein passage through the nuclear envelope pore complexes, i.e., the nuclear envelope regulates neither the number of potentially transportable ribosomal ribonucleoprotein particles in nuclei nor the number of those particles which can be maximally exported from nuclei at a given temperature. We suggest that these retention mechanisms involve temperature-sensitive domains of the nuclear matrix.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Wunderlich, F.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Giese, G.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Speth, V.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">782(1984), 2, Seite 187-194</subfield><subfield code="w">(DE-627)NLEJ176932224</subfield><subfield code="w">(DE-600)2209522-6</subfield><subfield code="x">0167-4781</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:782</subfield><subfield code="g">year:1984</subfield><subfield code="g">number:2</subfield><subfield code="g">pages:187-194</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0167-4781(84)90023-X</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">782</subfield><subfield code="j">1984</subfield><subfield code="e">2</subfield><subfield code="h">187-194</subfield></datafield></record></collection>
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