Factor required for mammalian spliceosome assembly is localized to discrete regions in the nucleus

Fu, Xiang‐Dong; Maniatis, Tom

doi:10.1038/343437a0

Cited by 694 publications

(630 citation statements)

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“…The bn2-containing aggregates were reminiscent of the speckles in which splicing factors are concentrated (15)(16)(17). One splicing factor widely used for the detection of speckles is SC35 (16)(17)(18).…”

Section: Resultsmentioning

confidence: 99%

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Basonuclins 1 and 2, whose genes share a common origin, are proteins with widely different properties and functions

Vanhoutteghem

Djian

2006

Proc. Natl. Acad. Sci. U.S.A.

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Basonuclin (bn) 1 possesses three separated pairs of zinc fingers and a nuclear localization signal. It is largely confined to the basal cells of stratified squamous epithelia and to reproductive germ cells. bn1 can shuttle between the nucleus and the cytoplasm, and its location is correlated with the proliferative potential of the cell. The recently discovered bn2 also possesses three separated pairs of zinc fingers and a nuclear localization signal. Conservation of the zinc fingers and the nuclear localization signal by bn1 and bn2 indicates a common origin. However, in contrast to bn1, bn2 is found in virtually every cell type and is confined to the nucleus. Bn2 but not bn1 colocalizes with SC35 in nuclear speckles and, therefore, is likely to have a function in nuclear processing of mRNA.RNA processing ͉ speckles ͉ zinc fingers B asonuclin (bn1) is a zinc finger protein with highly restricted tissue distribution: It is found mainly in basal keratinocytes of stratified squamous epithelium and in reproductive germ cells (1-5). bn1 possesses three separated pairs of zinc fingers, a nuclear localization signal (NLS) and a serine-rich region that has been called the serine stripe (1). Although the evidence is not conclusive, it seems that the function of bn1 is related to the potential for cell proliferation (6). The only known function of bn1 is that of a transcription factor in the synthesis of ribosomal RNA (7, 8), but it is possible that bn1 possesses a nucleoplasmic function in the regulation of expression of genes transcribed by RNA polymerase II (9).A gene encoding a second basonuclin (bn 2) recently has been discovered (10, 11). Although the deduced amino acid sequences of bn1 and bn2 are only slightly Ͼ40% identical, bn2 possesses all of the characteristic features of bn1 described above. The bn2 mRNA is abundant in cell types that possess bn1 but is also found in tissues that lack bn1, such as kidney, intestine, and uterus. The genes for bn1 and bn2 differ greatly in size and are located on different chromosomes, but it is clear that they have a common evolutionary origin. The evolutionary conservation of bn2 is much greater than that of bn1. It has been postulated that the gene for bn2 is the older of the two. After its duplication, the gene for bn1 was free to evolve in other directions, whereas the gene for bn2 remained virtually invariant (9, 11).Previous work on immunocytological detection of bn1 was carried out with polyclonal antisera raised against most or all of the bn1 protein (6, 12). In view of the similarities between bn1 and bn2, it was possible that these antisera did not distinguish between the two basonuclins. To detect each basonuclin independently, we generated antibodies to specific determinants not shared by bn1 and bn2. Using these antibodies, we show that, although the two basonuclins are of common origin, they possess widely different functions, because bn2 is likely to have a function in pre-mRNA processing. ResultsEvolutionary Conservation of bn2. We had reported that bn2 was e...

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Section: Resultsmentioning

confidence: 99%

“…One splicing factor widely used for the detection of speckles is SC35 (16)(17)(18). Keratinocytes were double-stained with either the anti-bn1 or anti-bn2 antibody and with a monoclonal antibody to SC35.…”

Section: Resultsmentioning

confidence: 99%

Basonuclins 1 and 2, whose genes share a common origin, are proteins with widely different properties and functions

Vanhoutteghem

Djian

2006

Proc. Natl. Acad. Sci. U.S.A.

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“…Alignment of green and red signals resulted in yellow fluorescence (Figure 2b), which could be clearly distinguished under the microscope but could not be reproduced with fidelity in the photographic print because of the strong blue DAPI staining which resulted in an off-color whitishyellow staining of the speckles. SC-35 is known to be localized in the spliceosomal compartment of the nucleus (12). This subnuclear compartment contains many antigens, such as snRNPs, non-snRNP splicing factors, and nuclear matrix proteins.…”

Section: Resultsmentioning

confidence: 99%

High frequency of autoantibodies to insoluble cellular antigens in patients with chronic fatigue syndrome

Mikecz

Konstantinov

Buchwald

et al. 1997

Arthritis & Rheumatism

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Objective. To elucidate the humoral immune response in patients with chronic fatigue syndrome (CFS), by identification and characterization of autoantibodies.Methods. Initial immunofluorescence histochemistry studies of sera using human HEp-2 cell substrate were followed by antibody class subtyping and colocalization studies with reference antibodies. Association of CFS autoantigens with insoluble cellular components was determined by in situ extraction of soluble components and subsequent immunofluorescence histochemistry studies on the extracted cell substrate.Results. Of 60 CFS patients, 41 (68%) were positive for antinuclear antibodies. Localization of nuclear staining was found at the nuclear envelope (52%), in reticulated speckles (25%), in nucleoli (13%), and in dense fine speckles (5%). Twenty-eight CFS sera (47%) also had antibodies to cytoplasmic antigens. The major cytoplasmic staining pattern was of the intermediate filament type (35%). The observed nuclear envelope pattern of staining co-localized with lamina-associated polypeptide 2 (an integral nuclear membrane protein), the reticulated speckle pattern co-localized with nonsmall nuclear RNP splicing factor SC-35, and the Publication no. 9865MEM from The Scripps Research Institute.

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“…For affinity purification of PAB II-specific antibodies, 10 /.tg of purified PAB II was loaded onto a SDS~polyacrylamide gel and transferred to nitrocellulose. The hlot was stained with Ponceau S, and the band of PAB 11 was cut out and used for affinity purification according to (91. Other antibodies used in this study were a monocional antibody (3A7) directed against the 64-kDa subunit oftbe human cleavage stimulation factor [10], a monoclonal antibody against the splicing factor SC-35 [11], p80 coilin-specific buman autoimmune serum (a gift from Dr. A. Lamond), anti-Sm human autoimmune serum (Küng) [12], and a monoclonal antibody (IGElO) against human PAB I [13].…”

Section: Methodsmentioning

confidence: 99%

Immunodetection of Poly(A) Binding Protein II in the Cell Nucleus

Krause

Fakan

Weis

et al. 1994

Experimental Cell Research

116

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During the polyadenylation of pre-mRN A in vitro~ poly(A) binding protein 11 (PAB 11) bind. to tbe growing poly(A) taH, stimulating its extension. Tbe subcellular localization of PAß 11 was investigated witb an antibody affinity-purified from rabbit serum raised against the purified protein. Immunoßuorescence microscopy detected PAß 11 exclusively in tbe cell nueleus, botb in a widespread staining and in more intensely stained "speckles." PAß 11 was excluded from the nucleoli. ßy electron microscopy, PAß II was also found almost exclusively in the nucleus, predominantly in clusters of interchromatin granules, likely corresponding to the speckles observed by immunofluorescence microscopy, and in perichromatin fibrils, wbich represent nascent transeripts and probably tbe sites of pre-mRN A processing. In addition, electron microscopy also detected P AB 11 in nucleoli. Tbe distribution corresponds largely to that of other factors involved in the processing of premRNA and is thus in agreement witb the proposed role of the protein in polyadenylation.

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Factor required for mammalian spliceosome assembly is localized to discrete regions in the nucleus

Cited by 694 publications

References 38 publications

Basonuclins 1 and 2, whose genes share a common origin, are proteins with widely different properties and functions

Basonuclins 1 and 2, whose genes share a common origin, are proteins with widely different properties and functions

High frequency of autoantibodies to insoluble cellular antigens in patients with chronic fatigue syndrome

Immunodetection of Poly(A) Binding Protein II in the Cell Nucleus

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