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G Herlan

Publications and source records attributed to G Herlan.

7 recordsLinked to original sources
PubMed1984

Thermal down-regulation of exportable rRNA in nuclei.

The export of rRNP particles from nuclei isolated from Tetrahymena was investigated after preincubating the nuclei at different temperatures under nonpermissive export-conditions. We observed a new phenomenon: Temperature elevation from the sublethal cells' growth temperature, 8 degrees C, to the optimal temperature, 28 degrees C, lead to a gradual down-regulation in the maximal proportion of rRNP particles subsequently exported from nuclei at 28 degrees C. This thermal down-regulation is apparently not due to qualitative changes in the exported rRNP particles, a derangement in the gross nuclear organization, a degradation and/or nicking of the nuclear rRNA, a gross decomposition of the major nuclear proteins, a random cross-linking of nuclear components by disulfide bonds, or an elution of nuclear factors possibly required for rRNP export. Moreover, there is a corresponding thermal down-regulation in nuclear envelope-free nuclei. Our data indicate that nuclei possess a mechanism that regulates the number of potentially exportable rRNP particles at a level preceding the rRNP passage through the nuclear envelope.

Animals↗
PubMed1980

In vitro ribosomal ribonucleoprotein transport upon nuclear expansion.

The interdependence of nuclear rRNA release and nuclear size is investigated in macronuclei isolated from Tetrahymena. Nuclei are induced to contract and to expand, without any structural disintegration of the nuclear envelope, by final Ca2+/Mg2+ (3:2) concentrations of 5 and 1.5 mM, respectively. Upon expansion, the average volume of nuclei increases from 600 +/- 42 to 811 +/- 76 micron3. Concomitantly, nuclei begin to release RNA following saturation kinetics. This RNA release stops immediately upon nuclear contraction. Similar to the in vivo situation, only advanced rRNA processing products are released in the form of ribosomal precursor particles, as identified in detail by polyacrylamide gel electrophoresis and rate zonal and isopycnic density gradient centrifugation. Three particle ty9es are released having average buoyant densities of 1.495, 1.470, and 1.532 g/cm3, exhibiting average sedimentation coefficients of 62, 62, and 35 S, and containing the immediate precursor to the 25S rRNA, 26S rRNA, and 17S rRNA, respectively. Tje rRNP release if ATP independent and noncoincident with the release of endogenous nuclear Pi, though it is Be2+ sensitive. Our data are compatible with the views that nuclear expansion is the prerequisite rather than the cause for the rRNP release and that nuclear pore complex associated ATPases play only, if at all, a minor role in nucleocytoplasmic exchange of rRNP.

Animals↗
PubMed1977

Reversibly contractile nuclear matrix. Its isolation, structure, and composition.

From Tetrahymena macronuclei we have isolated a reversibly contractile nucleo-skeleton, i.e., an "expanded" nuclear matrix which reversibly contracts when the total concentration of the bivalent cations, Ca and Mg (3:2), is decreased to 5 mM or increased to 125 mM. During contraction the average diameter of the expanded matrix becomes reduced by about 24%; this corresponds to a volume contraction of about 55%. The reversible contraction of the nuclear matrix does not depend on ATP and cannot be inhibited by salygran. The expanded matrix is obtained by removing carefully from the macronuclei 89.7% of the phospholipid, 99.6% of the DNA, 98.5% of the RNA, and 74.8% of the protein by treatment with Triton X-100 and digestion with DNase and RNase followed by an extraction with 2 M NaCl. Electron microscopy reveals, within the expanded matrix, residual equivalents to the structures characteristic for macronuclei: (a) a residual nuclear envelope with nuclear pore complexes; (b) residual nucleoli at the periphery; (c) a fibrillar internal network. The expanded matrix is essentially composed of proteins (96.2%) and traces of DNA (0.8%), RNA (0.5%), phospholipid (1.6%), and carbohydrates (0.9%). The last, which have been determined by gas chromatography, contain glucose, mannose, and an unidentified sugar in the ratio 1:5.4:5.7. The ratio of acidic to basic amino acids of the expanded matrix is 1.55. Sodium dodecyl sulfate (SDS) gel electrophoresis reveals a predominant protein with a mol wt of 18,000 which is apparently involved in the reversible contractile process. The mechanism of this reversible contraction of the expanded matrix remains to be elucidated, but it differs both from actin-myosin contraction systems and from the contractile spasmoneme system in vorticellids.

Calcium↗