A purified complex from <i>Xenopus</i> oocytes contains a p47 protein, an in vivo substrate of MPF, and a p30 protein respectively homologous to elongation factors EF‐1γ and EF‐1β

Bellé, Robert; Derancourt, Jean; Poulhe, Robert; Capony, Jean‐Paul; Ozon, René; Mulner‐Lorillon, Odile

doi:10.1016/0014-5793(89)81069-5

Cited by 69 publications

(14 citation statements)

References 24 publications

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“…The proteins known to be present in the nucleus include the homologue of targeting protein for Xenopus kinesin-like protein 2 (Xklp2) (TPX2, AF244547) (44 -46, 56 -58) and the p32cdc2-like PITSLRE protein kinase ␣ SV9 isoform (AF080683) (47,60). The other non-ribosomal proteins we identified are fibronectin (48,49), tubulin ␣1, putative (AK01960, ␤-tubulin isotype M-␤ 5), growth arrest specific 11 (50,51), putative (AK007869, eukaryotic translation elongation factor 1) (52,53,59), putative (AK010776), and GAJ (Supplementary Table III). All of these non-ribosomal proteins except GAJ and putative (AK010776) can be categorized coincidentally into protein factors participating or expected to be participating in microtubule assembly or nucleologenesis occurring during the M-phase of the cell cycle (Table II and Supplementary Table III).…”

Section: Resultsmentioning

confidence: 99%

Isolation and Proteomic Characterization of Human Parvulin-associating Preribosomal Ribonucleoprotein Complexes

Fujiyama

Yanagida²,

Hayano³

et al. 2002

Journal of Biological Chemistry

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Human parvulin (hParvulin; Par14/EPVH) belongs to the third family of peptidylprolyl cis-trans isomerases that exhibit an enzymatic activity of interconverting the cis-trans conformation of the prolyl peptide bond, and shows sequence similarity to the regulator enzyme for cell cycle transitions, human Pin1. However, the cellular function of hParvulin is entirely unknown. Here, we demonstrate that hParvulin associates with the preribosomal ribonucleoprotein (pre-rRNP) complexes, which contain preribosomal RNAs, at least 26 ribosomal proteins, and 26 trans-acting factors involved in rRNA processing and assembly at an early stage of ribosome biogenesis. Since an amino-terminal domain of hParvulin, which is proposed to be a putative DNA-binding domain, was alone sufficient to associate in principle with the pre-rRNP complexes, the association is probably through protein-RNA interaction. In addition, hParvulin co-precipitated at least 10 proteins not previously known to be involved in ribosome biogenesis. Coincidentally, most of these proteins are implicated in regulation of microtubule assembly or nucleolar reformation during the mitotic phase of the cell. Thus, these results, coupled with the preferential nuclear localization of hParvulin, suggest that hParvulin may be involved in ribosome biogenesis and/or nucleolar re-assembly of mammalian cells.

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Section: Resultsmentioning

confidence: 99%

Isolation and Proteomic Characterization of Human Parvulin-associating Preribosomal Ribonucleoprotein Complexes

Fujiyama

Yanagida²,

Hayano³

et al. 2002

Journal of Biological Chemistry

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“…Further studies are underway to elucidate the exact function of EF-16 in complex formation with EF-1Py. It is interesting to note that in Xenopus oocytes a 47-kDa protein, resembling EF-ly, is a substrate for the cdc2 kinase [20]. This protein in Xenopus is part of a protein complex which contains also functionally active EF-lP and EF-16 (R. Belle and W. Moller, unpublished results).…”

Section: Discussionmentioning

confidence: 99%

Mapping the functional domains of the eukaryotic elongation factor 1βγ

Damme¹,

Amons²,

Janssen³

et al. 1991

European Journal of Biochemistry

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The functional domains of the eukaryotic elongation factor (EF) 1Py have been delineated with the use of limited proteolysis, protein microsequencing, gel electrophoresis under non-denaturing conditions and antibodies against EF-1P and EF-ly. By means of limited proteolysis, it was possible to obtain large fragments of EF-ID. In contrast to amino-terminal fragments, those derived from the carboxy-terminal part of EF-ID were still active in enhancing the guanine nucleotide exchange of GDP bound to EF-la. With the same technique of limited proteolysis, it was possible to isolate a trypsin-resistant core from EF-1 By containing polypeptide chain fragments derived from both subunits. A polyvalent antiserum against EF-1P and two monoclonal antibodies against EFl y were used to identify the protein fragments in this core. The monoclonal antibodies were shown to recognize different epitopes, one localized on the amino-terminal and another on the carboxy-terminal half of EF-I y. The antiserum against EF-1P and one of the monoclonal antibodies (mAb 36E5), which recognized the amino-terminal half of EF-ly, reacted with this trypsin-resistant core. We conclude that the amino-terminal halves of both EF-IB and EF-ly are firmly attached to each other, and that the carboxy-terminal part of EF-lP interacts with EF-la.Protein synthesis requires factors for proper translation [I]. In prokaryotes, correct binding of aminoacyl tRNA to translating ribosomes is mediated by elongation factor EFTu, a protein which is able to form a ternary complex with aminoacyl tRNA and GTP. Under simultaneous hydrolysis of GTP into GDP and Pi, the cognate aminoacyl tRNA becomes bound to the ribosome mRNA complex [2]. Replacement of GDP, in the EF-Tu . GDP complex, by GTP is enhanced by a separate factor, EF-Ts, the nucleotide-exchange factor [2]. The situation in eukaryotes is similar; here, however, EF-I a ( Z 50 kDa) replaces EF-Tu, whereas a complex between two polypeptide chains, EF-1fi and EF-ly, functions as the nucleotide-exchange factor [2]. The actual exchange activity, which resides on EF-lP (~2 6 kDa), is modulated by phosphorylation of its residue Ser89 [3]. The role of EF-ly (~4 6 kDa), a protein with strong hydrophobic properties, is not yet clear, although it possesses a stimulating effect on the exchange activity of EF-1P [4]. High-molecular-mass complexes between EF-la and EF-1Py have been described in many eukaryotic tissues [5 -111.In an attempt to unravel the requirements for nucleotideexchange activity and the involvement of the protein stretch around the phosphorylated residue Ser89 in EF-IP, we have isolated large, well-defined proteolytic fragments of this pro- Abbreviations. EF-la, EF-Ib, EF-Iy and EF-16, the a, b, y and 6 subunits of the eukaryotic protein synthesis elongation factor 1 ; EFTu, prokaryotic equivalent of the eukaryotic protein synthesis elongation factor 13; EF-Ts, prokaryotic equivalent of the eukaryotic protein synthesis elongation factor 1 f l y ; mAb, monoclonal antibody.Enzymes. Trypsin (EC 3.4.21.4); clo...

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“…Phosphorylation of eEF-la, eEF-lP and eEF-ly has been reported [191,192,292]. Thephosphorylation ofeEF-la seems to alter the ribosomal binding properties of the factor as isolated ribosomes do not contain any phosphorylated factor [191].…”

Section: Regulation Of the Activity Of Eef-imentioning

confidence: 99%

“…aminoacyl-tRNA complexes. eEF-1 y is phosphorylated by a cell-division-controlled protein kinase ~3 4~~" ' [292]. The functional role of this modification is not yet known, but the phosphorylation seems to correlate with the changes in protein synthesis activity during cell division.…”

Section: Regulation Of the Activity Of Eef-imentioning

confidence: 99%