Characterization by human antibodies of two HeLa cell proteins which are related to<i>Xenopus laevis</i>transcription factor TFIIIA

Lagaye, Sylvie; Barque, Jean-Philippe; Maire, Marc le; Denis, Hélène; Larsen, Christian‐Jacques

doi:10.1093/nar/16.6.2473

Cited by 12 publications

(4 citation statements)

References 23 publications

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“…Autoantibodies to RNAP I, II and Ill are relatively common (5-10). Although less common, several examples of autoantibodies specific for RNAP I and RNAP Ill accessory factors have been reported, including anti-NOR 90 antibodies, which react with the RNAP I factor hUBF (11,12), antibodies reactive with proteins related to TFIIIA (13), and anti-La antibodies, which react with a factor required for accurate RNAP Ill transcription (14,15). To our knowledge, however, there are no reports of autoantibodies to RNAP II accessory factors, nor have there been systematic efforts to identify such antibodies.…”

Section: Introductionmentioning

confidence: 99%

Identification of human autoantibodies to transcription factor IIB

et al. 1995

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We have characterized the ability of various human autoimmune sera to react with RNA polymerase II transcription factors. One serum, which strongly inhibited transcription in a cell-free system, was shown to contain antibodies directed against human TFIIB. The serum did not show reactivity against the other general transcription factors, including human TBP, TFIIE and TFIIF. The inhibition of transcription was directly attributable to depletion of TFIIB activity, as demonstrated by reconstitution of activity with recombinant TFIIB. It has long been recognized that components of the RNA processing machinery are major human autoantigens. The present results show that at least one general transcription factor required for messenger RNA synthesis is an autoantigen as well.

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Section: Introductionmentioning

confidence: 99%

Identification of human autoantibodies to transcription factor IIB

et al. 1995

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“…If 5S rRNA enters the nucleus in excess of the amount required for assembly into nascent 60S ribosomal subunits, it may become associated with TFIIIA. Along these lines, it has been proposed that excess 5S rRNA may be targeted to the cytoplasm of mammalian somatic cells for degradation bound to a TFIIIA-like protein (39).…”

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confidence: 99%

Structural requirements of 5S rRNA for nuclear transport, 7S ribonucleoprotein particle assembly, and 60S ribosomal subunit assembly in Xenopus oocytes.

Allison¹,

North²,

Murdoch³

et al. 1993

Mol. Cell. Biol.

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Structural requirements of 5S rRNA for nuclear transport and RNA-protein interactions have been studied by analyzing the behavior of oocyte-type 5S rRNA and of 31 different in vitro-generated mutant transcripts after microinjection into the cytoplasm of Xenopus oocytes. Experiments reveal that the sequence and secondary and/or tertiary structure requirements of 5S rRNA for nuclear transport, storage in the cytoplasm as 7S ribonucleoprotein particles, and assembly into 60S ribosomal subunits are complex and nonidentical. Elements of loops A, C, and E, helices II and V, and bulged and hinge nucleotides in the central domain of 5S rRNA carry the essential information for these functional activities. Assembly of microinjected 5S rRNA into 60S ribosomal subunits was shown to occur in the nucleus; thus, the first requirement for subunit assembly is nuclear targeting. The inhibitory effects of ATP depletion, wheat germ agglutinin, and chilling on the nuclear import of 5S rRNA indicate that it crosses the nuclear envelope through the nuclear pore complex by a pathway similar to that used by karyophilic proteins.The orchestration of ribosome biogenesis in eukaryotic cells is a process that requires transfer of macromolecules into and out of the nucleus. In Xenopus oocytes, 5S rRNA is shuttled between the nuclear and cytoplasmic compartments of the oocyte during different stages of oogenesis in a complex pathway involving different protein associations. In previtellogenic oocytes, 5S rRNA is synthesized before other components of ribosomes are available, is exported from the nucleus, and stored in the cytoplasm as 7S ribonucleoprotein particles (RNPs) (5S rRNA complexed with transcription factor IIIA [TFIIIA]) or as 42S RNPs (5S rRNA complexed with other nonribosomal proteins and tRNA). During vitellogenesis, the 5S rRNA is released from storage and a 5S rRNA-ribosomal protein L5 complex, which is a precursor to assembly into the 60S large ribosomal subunit, forms (reference 3 and references therein). We are interested in the mechanisms that govern the subcellular trafficking of 5S rRNA within the oocyte, particularly the requirements for the mobilization of stored 5S rRNA during ribosome assembly.There nuclear RNAs (50), mRNA (16), 40S and 60S ribosomal subunits (6, 38), and 5S rRNA (24) occurs in a manner consistent with a mediated process. Analysis of the nuclear transport of U small nuclear RNAs has multiple defined, kinetically distinct targeting pathways (27,47,48). Nuclear transport of different classes of RNA may thus involve targeting to the pore complex by different cytoplasmic receptors and then translocation into the nucleus by the same pore complex-mediated mechanism. Specific RNA structures have been implicated as requirements for both nuclear import and export (5,22,32,33,67,75). Translocation of RNA molecules across the nuclear envelope may also require interaction with specific proteins (28,31,33,43,62). RNA-protein interactions are important for many regulatory processes. There is growing evidence that R...

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“…Only oocytes accumulate large amounts of this protein (Shastry et al 1984). Somatic cells contain only trace amounts of TFIIIA, and presumably use it as a housekeeping factor (Lagaye et al 1989). Likewise, nonlens cells use some crystallins as plain enzymes (de Jong et al 1989).…”

Section: Gene Diversion In the Family Of Oocyte Rna-binding Proteinsmentioning

confidence: 99%

Origin of several abundant proteins of amphibian oocytes

1992

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Previous studies indicate that the genes controlling cell-specific functions in extant metazoans derive from housekeeping genes of their unicellular ancestors. Traces of such relationships can be found in the gene families controlling signal reception at cell surfaces and light condensation in eye lens. We present other examples of gene remodeling taken in the field of germ cell-specific proteins. In amphibian oocytes several proteins contribute to edification of an efficient translation machinery for the future embryo. Some RNA components of this machinery have to be protected against degradation during growth of the oocytes in the ovary. The protective function is served by a small group of RNA-binding proteins deriving from universal transcription or translation factors. Several of those proteins are bifunctional.

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Characterization by human antibodies of two HeLa cell proteins which are related toXenopus laevistranscription factor TFIIIA

Cited by 12 publications

References 23 publications

Identification of human autoantibodies to transcription factor IIB

Identification of human autoantibodies to transcription factor IIB

Structural requirements of 5S rRNA for nuclear transport, 7S ribonucleoprotein particle assembly, and 60S ribosomal subunit assembly in Xenopus oocytes.

Origin of several abundant proteins of amphibian oocytes

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