Cordes VC , Reidenbach S , Rackwitz HR , Franke WW .

GM26514 NIGMS NIH HHS

	Figure 2. Immunoblot detection of a ∼270-kD mammalian protein reactive with mAb 203-37. Proteins were separated by SDS-PAGE and then, in parallel, either stained by Coomassie blue (a, b, and c) or transferred to nitrocellulose filters for immunodetection of proteins (a′, b′, and c′) by enhanced chemiluminescence reaction (ECL). Same amounts of protein were loaded in corresponding lanes of gels for Coomassie staining and immunoblotting. (a) Separation of total proteins from HeLa cells and (a′) immunoblot detection of a ∼270-kD protein, p270, immunoreactive with mAb 203-37. (b and b′) Fractionation of HeLa cells and immunoblot detection of p270 in a residual detergent and salt-resistant fraction: Hela cells were first extracted with 0.2% Triton X-100 (lanes 1), washed with detergent-free buffer (lanes 2), extracted with 500 mM NaCl (lanes 3), and washed with nearly salt-free buffer (lanes 4). The residual cyto- and karyoskeletal proteins were separated in lanes 5. Gels were loaded with the same percentage of proteins from each fraction. Note that the major proportion of p270 remains structure-associated after detergent and intermediate ionic strength-salt treatment. A certain amount of intact p270 has been released into solution by salt extraction as well as putative degradation products (marked by a bracket in b′). In contrast to protein p270, a weakly immunoreactive polypeptide of ∼75 kD, visible after prolonged film exposure (not shown) in the residual cyto- and karyoskeletal fraction (lane 5), was not detected after application of more stringent filter washing conditions (see Materials and Methods). (c and c′) Separation of total proteins from porcine kidney cells of line PK(15) (lanes 1) and bovine mammary gland epithelial cells of line BMGE (lanes 2) and immunoblot detection of protein p270 with mAb 203-37 also in these species. Relative molecular masses of marker proteins (M) in a–c (denoted by dots at the left margin in a′–c′) are, from top to bottom, as follows: 205, 116, 97, 66, 45, and 29 kD.
	Figure 3. Immunoelectron microscopy of mammalian cells and tissues using mAb 203-37 in a preembedding technique, showing intense decoration of intranuclear sites near NPCs, often directly seen on the NPC-associated intranuclear filaments. Immunogold localization (5-nm gold–coupled secondary antibodies) of protein p270 on cryostat sections of human liver (a–c), bovine testis (d and e), and in detergent-permeabilized human PLC cells (f). Cross-sections presented in a–e reveal exclusive labeling at the nucleoplasmic side of the NPC and on the NPC-attached filaments extending into the nuclear interior. The grazing section presented in f allows insight into the nuclear interior (N), and reveals nucleoplasmic labeling of two NPCs or its associated filament bundles (short thick arrows) whereas no labeling is observed at the level of the outer, i.e., cytoplasmic annulus or in the mid-plane of the NPCs as demonstrable by the presence of a dense central granule (long thin arrows). (g–j) Double label immunogold EM on cryostat sections of human (g) and bovine (h–j) liver using mAb 203-37 (5-nm gold–coupled secondary antibodies) and affinity-purified guinea pig (g, gp-αRBP2-2) and rabbit antibodies (h–j, rb-αRBP2-2) against RanBP2/Nup358 (10-nm gold–coupled secondary antibodies); RanBP2 representing a marker protein for the cytoplasmic side of the NPC. Cryostat sections were fixed with acetone (a, c, and h–j) or formaldehyde (b, d, e, and g). PLC cells were fixed with formaldehyde and then permeabilized by digitonin treatment (f). N, nuclear interior. C, cytoplasmic side. The outer nuclear membrane (denoted o in some figures) is oriented to the top in a–e and g–j. Thin long arrows in some figures mark several NPCs at their cytoplasmic side; thicker and shorter arrows denote immunoreactive intranuclear filamentous material at or near NPCs. Bars: (a–d, f–h) 0.1 μm; same magnification in d and e, and in h and i; (g) 0.05 μm; (j) 0.2 μm.
	Figure 4. Characterization of p270 cDNA clones isolated from a human expression library using mAb 203-37. (a) Schematic presentation of human p270 cDNA clones isolated from a fetal brain Uni-ZapTMXR cDNA library. Screening of this library with mAb 203-37 yielded one clone (T1: bp 1-7321) containing the entire coding region (bp 89-7177) for human Tpr, and five partial Tpr cDNA clones (T2: bp 2374-7321; T3: 2723-7321; T4: 2825-7321; T5: 3505-7321; T6: 3880-7321; lengths of polyA-tails varied between different clones and were omitted in the context of this bp numbering). The position of the AUG start codon in clone T1 is indicated by a circle, the stop codon present in all clones by squares. The ORF of T1 encodes a 2,363–residue protein with a predicted molecular mass of 267,333 D. Clones T3 and T4 represent fusion clones that also contain unrelated nt sequences at their 3′ end (not shown). Arrows denote the relative position of a sequence insertion, present in all clones, that occurs in addition to the previously published amino acid (aa) sequence of human Tpr and results in a prolonged acidic aa cluster (see b). The scale corresponds to the nt sequence of T1, each calibration line representing 1 kb. (b) An additional acidic aa sequence segment in human fetal brain Tpr. The top line shows the previously published aa sequence of human Tpr deduced from cDNA clones isolated from fibroblast and fibrosarcoma cDNA libraries (Mitchell and Cooper, 1992a,b). The bottom line shows the sequence of human fetal brain Tpr, containing 14 additional, mainly acidic aa. (c) Radiolabeled products obtained by in vitro transcription-translation of human Tpr cDNA clone T1 in reticulocyte lysate. The product with the lowest mobility (arrowhead) corresponds to a relative molecular mass of 270 kD. Radiolabeled polypeptides of lower relative masses may represent proteolytic products of Tpr or translation products resulting from misuse of sequence-internal AUG codons as translation initiation sites. Relative masses of reference proteins (positions denoted by dots on the left) are, from top to bottom, as follows: 205, 116, 97, 66, 45, and 29 kD. (d) Immunoprecipitation of radiolabeled human Tpr protein. In vitro translation products of cDNA clone T1 were incubated with protein G–Sepharose alone (lane 1) or together with mAb 203-37 (lane 2). Note that immunoabsorption of human Tpr from the reticulocyte lysate occurs only in the presence of mAb 203-37. Relative masses of reference proteins (dots on the left) are as in (c). (e–g′) Immunofluorescence microscopy on African green monkey kidney cells transfected with an expression vector encoding human fetal brain Tpr. Cells were stained with mAb 203-37 reactive with human Tpr, in transfected cells, but not with the endogenous monkey orthologue of Tpr. The same fields are shown in phase contrast (e–g) and epifluorescence optics (e′–g′). Besides a finely punctate nuclear labeling, reminiscent of NPC staining, intranuclear reaction sites are also noticeable. In a few transfected cells immunoreactive dots are located near the nucleoli (arrows in f–g′; compare also with Fig. 7, f–g′). Cells were fixed with methanol/acetone. Bars, 10 μm.
	Figure 7. Immunofluorescence microscopy of cultured cells and tissue cryostat sections after reaction with affinity-purified guinea pig and rabbit antibodies raised against different epitopes of human and Xenopus Tpr. (a) HeLa cells stained with guinea pig antibodies against hTpr-Pep1 (gp-αhTpr-Pep1). (b) Bovine mammary gland epithelial cells of line BMGE stained with rabbit antibodies against hTpr-Pep2 (rb-αhTpr-Pep2). (c and d) Cryostat section of human epidermis (c) stained with gp-αhTpr-Pep1 and human esophagus (d) stained with rb-αhTpr-Pep2. Note that the nuclear staining obtained with these antibodies is essentially indistinguishable from that obtained with mAb 203-37 (see Fig. 1). In addition to the finely punctate nuclear staining resembling immunolabeling of NPCs, immunoreactive intranuclear dots are also observed occasionally (a and b). (e–g′) Xenopus laevis kidney epithelial cells stained with rabbit antibodies against xlTpr-Pep3 (rb-αxlTpr-Pep3). In addition to the finely punctate nuclear labeling, intranuclear dots are noticed in a minor proportion of cells in which they sometimes appear to surround the nucleoli (f–g′). (h and h′) Cryostat sections through a Xenopus oocyte stained with rb-αxlTpr-Pep3. Epifluorescence (a–e; f′, g′, and h′) and corresponding phase contrast optics (f, g, and h) are shown. Cultured cells were fixed with methanol/acetone (a, e–g′) or formaldehyde followed by detergent treatment (b). Cryostat sections were fixed with formaldehyde (c) or acetone (d and h). N, nucleus. Bars: (a and e) 20 μm; same magnification in b; (c) 50 μm; same magnification in d; (g) 10 μm; same magnification in f; (h′) 100 μm.
	Figure 5. Immunoblot detection of p270 with affinity-purified guinea pig and rabbit antibodies raised against human Tpr protein. (a) Schematic presentation of human protein Tpr and the relative positions (arrows) of the two Tpr peptides, No. 1 (hTpr-Pep1, 1.) and No. 2 (hTpr-Pep2, 2.), against which antibodies were raised. The hatched box designates the amino-terminal domain of Tpr predicted to form α helices capable of forming coiled-coil structures. The carboxy-terminal domain (black line) is characterized by several acidic regions. The major cluster of acidic aa (corresponding to the cluster shown in Fig. 4 b) is designated by an open circle. Basic sequence elements (not denoted) separate the acidic regions and also characterize the ∼50–carboxy-terminal aa. (b–b‴) SDS-PAGE of total HeLa cell proteins separated into a fraction of soluble proteins released by digitonin permeabilization of cells (lanes 1) and of residual, nonextracted proteins (lanes 2). Proteins were, in parallel, either stained by Coomassie blue (b) or transferred to nitrocellulose for immunodetection of proteins by ECL (b′–b‴). Same amounts of proteins were loaded in corresponding lanes of gels for Coomassie staining and immunoblotting. Digitonin treatment of HeLa cells already triggered proteolytic breakdown of protein Tpr and was applied to analyze immunoreaction of degradation products with different Tpr peptide antibodies. (b′) Immunoblot using mAb 203-37 as reference, showing the detection of protein p270/Tpr and a major putative degradation product of ∼210-kD. (b″) Immunoblot using guinea pig antibodies against hTpr-Pep1 showing essentially the same result as obtained with mAb 203-37: besides predominant labeling of p270/Tpr, immunoreaction is also noticed with the ∼210-kD polypeptide. (b‴) Immunoblot using rabbit antibodies against hTpr-Pep2 showing labeling of p270/Tpr whereas the shorter degradation product of ∼210 kD is not immunoreactive. Note that hTpr-Pep2 is located nearer towards the protein's carboxy terminus than hTpr-Pep1. Relative masses of marker proteins (M) (denoted by dots in b′-b‴) are as in Fig. 2. (c–c″) Identification of p270 as protein Tpr by double immunoblotting with mAb 203-37 and rabbit antibodies raised against hTprPep2. Residual HeLa proteins obtained after digitonin extraction were separated by IEF and SDS-PAGE and then transferred to a nitrocellulose filter (2). As reference, the same protein fraction was also separated on the left side of the same gel by SDS-PAGE alone (1), together with marker proteins (denoted by dots in lanes M) with relative masses, from top to bottom, of 205, 116, 97, and 66 kD. The filter (only the upper half is shown) was first incubated with mAb 203-37 and HRP-coupled secondary antibodies to murine Ig (c): the immunoblot reaction (ECL procedure, exposure time <1 min) identifies p270 (arrow) and putative degradation products (brackets in 1 and 2) of ∼210 kD. Bound antibodies were then released under acidic conditions and the filter incubated solely with HRP-coupled secondary antibodies to rabbit Ig (c′): ECL (exposure time >12 h) reveals no unspecific immunoreaction of p270 with these secondary antibodies. The filter then again was washed in acidic buffer and incubated with affinity-purified rabbit antibodies raised against hTpr-Pep2 (rbαhTpr-Pep2) and HRP-coupled α-rabbit secondary antibodies: ECL (exposure time <1 min) shows specific labeling of protein Tpr (arrow). Note that proteins identified as p270 in c and as Tpr in c″ are indistinguishable by electrophoresis. As expected, the 210-kD putative degradation product is not immunoreactive with rb-αhTpr-Pep2.
	Figure 6. Generation of antibodies immunoreactive with amphibian Tpr. (a) Isolation of PCR products encoding the carboxy-terminal domain of the Xenopus laevis Tpr protein and alignment of human and Xenopus Tpr aa sequences. A Xenopus kidney cDNA library was used as template for PCR assays. Several overlapping DNA fragments were assembled into a partial DNA sequence of 1811 bp that encodes the 558–carboxy-terminal aa of Xenopus Tpr (p-xlTPR) shown in the bottom lane of the alignment; the corresponding human sequence is shown in the upper lane (hTPR). Numbers at the right margin stand for aa positions in accordance to full-length human fetal brain Tpr. Identical aa (bold letters) and homologous aa are boxed. Groups of homologous aa as relevant for this alignment were laid down as follows: R+K; D+E; S+T; V+A+P; V+I+L+M. (b) Schematic presentation of the partial Xenopus Tpr aa sequence (p-xlTPR) and the relative position (arrow) of a Xenopus Tpr peptide, xlTpr-Pep3 (3.), against which antibodies were raised. The human Tpr scheme (hTPR) with its relative peptide positions is shown as a reference. (c) Immunodetection of Xenopus protein p270/Tpr with affinity-purified rabbit antibodies raised against xlTpr-Pep3. Total proteins from Xenopus laevis kidney epithelial cells (lanes 1) and from manually isolated Xenopus oocyte nuclei (lanes 2) were separated by SDS-PAGE and, in parallel, either stained by Coomassie blue (c) or transferred to nitrocellulose for immunodetection of proteins by ECL (c′). Same amounts of protein were loaded in corresponding lanes of c and c′. Relative masses of marker proteins (M) in c (denoted by dots in c′) are as in Fig. 2.
	Figure 8. Double immunofluorescence microscopy of mammalian and amphibian cells using antibodies against p270/Tpr (a–c), and against other NPC proteins (a′–c′) that represent marker proteins for pore complexes both of the nuclear envelope and the cytoplasmic annulate lamellae. (a and a′) HeLa cells immunolabeled with mAb 203-37 against human Tpr (a) and affinity-purified guinea pig antibodies (gp-αRBP2-2) against RanBP2/Nup358 (a′). (b and b′) Bovine mammary gland epithelial cells of line BMGE immunolabeled with (b) affinity-purified rabbit antibodies against hTpr-Pep2 (rb-αhTpr-Pep2) and (b′) mAb 414 reactive with the XFXFG-family of O-glycosylated nucleoporins. (c and c′) Cryostat section through a Xenopus laevis stage VI oocyte immunolabeled with (c) affinity-purified rabbit antibodies against xlTpr-Pep3 (rb-αxlTpr-Pep3) and (c′) gp-αRBP2-2. Note that no cytoplasmic staining is detectable with Tpr-antibodies whereas distinctive cytoplasmic structures, representing annulate lamellae, are immunoreactive with antibodies against other NPC proteins. Secondary antibodies were coupled to cyanine 2-OSu bisfunctional (a and c′) or fluorescein isothiocyanate (b′) and cyanine 3.29-OSu (a′ and c) or Texas red sulfonyl chloride (b). Cultured cells were fixed with methanol/acetone (a and a′) or formaldehyde followed by detergent treatment (b and b′). The oocyte cryostat section was fixed with acetone (c and c′). Bars: (a and b) 15 μm; (c) 100 μm.
	Figure 9. Immunoelectron microscopy of human tissues after reaction with affinity-purified antibodies raised against different epitopes of human Tpr revealing exclusive intranuclear localization of protein p270/Tpr. (a–e) Immunogold localization (5-nm-gold) of p270/Tpr on cryostat sections of human liver using rabbit antibodies (rb-αhTpr-Pep2) against hTpr-Pep2 (a–c, and e) and guinea pig antibodies (gpαhTpr-Pep1) against hTpr-Pep1 (d). Thin long arrows in some figures mark several NPCs at their cytoplasmic side; thicker and shorter arrows denote immunoreactive intranuclear filaments. In addition to the immunolocalization of p270/Tpr in NPC-attached filamentous material, labelings of electron-dense spheroidal intranuclear structures (arrowheads in e) are occasionally observed. (f–h) Double label immunogold EM on cryostat sections of human liver confirming the exclusively intranuclear localization of protein p270/Tpr. (f and g) rb-αhTpr-Pep2 (5-nm-gold) and guinea pig antibodies (gp-αRBP2-2) against RanBP2/Nup358 (10-nm-gold). (h) gp-αhTpr-Pep1 (5nm-gold) and rabbit antibodies (rb-αRBP2-2) against RanBP2/Nup358 (10-nm-gold). Cryostat sections were fixed with acetone (a–g) or formaldehyde (h). N, nuclear interior. C, cytoplasmic side. The outer nuclear membrane (denoted o in some figures) is oriented to the top in all figures. Bars: (a–e) 0.2 μm, same magnification in a–d; (f–h) 0.1 μm; same magnification in g and h.
	Figure 10. Immunoelectron microscopy of Xenopus oocytes after reaction with affinity-purified antibodies raised against Xenopus p270/Tpr showing dense labeling of NPC-attached intranuclear filament bundles. (a–d) Immunogold localization (5-nm-gold) of Xenopus p270/Tpr on manually isolated nuclei using rabbit antibodies raised against xlTpr-Pep3 (rb-αxlTpr-Pep3). Note the exclusive localization of p270/Tpr in the intranuclear NPC-attached filament bundles that often appear laterally aggregated and partly entangled. An individual, nuclear envelope-attached annulate lamellae cisterna (AL, marked by a bracket in c) is devoid of gold grains. (e–k) Double label immunogold EM on manually isolated nuclei (e–j) and on a formaldehyde-fixed cryostat section through an oocyte (k) using rbαxlTpr-Pep3 (5-nm-gold) and guinea pig antibodies (gp-αRBP2-2) against RanBP2/Nup358 (10-nm-gold). Note that RanBP2 antibodies almost exclusively label the cytoplasmic side of the NPCs, whereas Tpr antibodies label intranuclear filaments. The grazing section through part of the nuclear envelope presented in i also shows the location of RanBP2 at the cytoplasmic side (C) of an NPC (long thin arrow), and Tpr at its nucleoplasmic (N) side. Note that protuberances extending from the corners of the NPCs eightfold symmetrical inner cylinder or annulus are labeled by Tpr antibodies (short thick arrows). Also, in h, intranuclear filaments extend far into the nuclear interior and occasionally interconnect nucleoli (No) and NPCs. Also note, in j, that cytoplasmic pore complexes of annulate lamellae, immunonegative for Tpr, are labeled by RanBP2 antibodies. Numbers of occasionally observed intranuclear 10-nm-gold grains and cytoplasmic 5-nm-gold were in the range of unspecific background labeling and secondary antibody cross-reactivities. The outer nuclear membrane (o) is oriented to the top in a–h and j–k. Thin long arrows in b mark several NPCs at their cytoplasmic side; thick short arrows denote intranuclear sites of Tpr labeling. M, mitochondria. Bars: (a–c, f–h, j, and k) 0.2 μm; (d and i) 0.1 μm, same magnification in d and e.

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