p19(super Skp1) and p45(super Skp2) are essential elements of the cyclin A-CDK2 S phase kinase
Article Abstract:
The cyclin A-cyclin-dependent kinase (CDK) 2, which in normal cells is associated with p21 and PCNA in quaternary complexes, in transformed cells is often present with cyclin A, CDK2, p9(super Skp1/Skp2), p19 and p45. The reason for this change is probably due to the large concentration of the protein p45 in transformed cells. The injection of antibodies or antisense oligonucleotides into normal and transformed cells inhibits the activity of p45 and prevents the entry of S phase of the cell cycle. Thus, the presence of p45 bound to cyclin A-CDK2 complexes is necessary for the replication of DNA.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Hedgehog elicits signal transduction by means of a large complex containing the kinesin-related protein costal2
Article Abstract:
A study was conducted of a protein complex that mediates signal transduction from a secreted protein (HH) encoded by the hedgehog gene of Drosophila melanogaster. The complex consists of the products of at least three genes: fused, cubitus interruptus and costal2. Great affinity was observed in the binding of the complex to microtubules in the absence of HH but binding is reversed by HH. The findings suggest that the complex may facilitate signalling from HH by governing access of the cubitus interruptus protein to the nucleus.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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Purification of Tetrahymena telomerase and cloning of genes encoding the two protein components of the enzyme
Article Abstract:
Purification of ciliate Tetrahymena telomerase by chromatography techniques revealed two protein subunits, 80 kDa (p80) and 95 kDa (p95), which copurified with telomerase activity, and the previously identified Tetrahymena telomerase RNA. Two-dimensional gel assay of the proteins showed similar polymerase activity between p80, p95 and the telomerase RNA. Coomassie staining of the proteins revealed a stoichiometry of 1:1:1 suggesting that p80 and p95 share some homology with the telomerase RNA.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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