Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors

de Vries H, Rüegsegger U, Hübner W, Friedlein A, Langen H, Keller W (2000)
The EMBO journal 19(21): 5895-5904.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
de Vries, H; Rüegsegger, U; Hübner, WolfgangUniBi ; Friedlein, A; Langen, H; Keller, W
Abstract / Bemerkung
Six different protein factors are required in vitro for 3' end formation of mammalian pre-mRNAs by endonucleolytic cleavage and polyadenylation. Five of the factors have been purified and most of their components cloned, but cleavage factor II(m) (CF II(m)) remained uncharacterized. We have purified CF II(m) from HeLa cell nuclear extract by several chromatographic steps. During purification, CF II(m) activity separated into two components, one essential (CF IIA(m)) and one stimulatory (CF IIB(m)) for the cleavage reaction. CF IIA(m) fractions contain the human homologs of two yeast 3' end processing factors, Pcf11p and Clp1p, as well as cleavage factor I(m) (CF I(m)) and several splicing and transcription factors. We report the cloning of hClp1 and show that it is a genuine subunit of CF IIA(m). Antibodies directed against hClp1 deplete cleavage activity, but not polyadenylation activity from HeLa cell nuclear extract. hClp1 interacts with CF I(m) and the cleavage and polyadenylation specificity factor CPSF, suggesting that it bridges these two 3' end processing factors within the cleavage complex.
Stichworte
RNA-Binding Proteins/genetics; RNA-Binding Proteins/chemistry; Fungal/metabolism; RNA; RNA Splicing; Post-Transcriptional; RNA Processing; RNA Precursors/metabolism; Protein Subunits; Molecular Sequence Data; Humans; HeLa Cells; Fungal Proteins/genetics; Fungal Proteins/chemistry; Molecular; Evolution; DNA Primers/genetics; Conserved Sequence; Amino Acid Sequence; Base Sequence; RNA-Binding Proteins/metabolism; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Sequence Homology; Amino Acid; Transcription; Genetic; mRNA Cleavage and Polyadenylation Factors
Erscheinungsjahr
2000
Zeitschriftentitel
The EMBO journal
Band
19
Ausgabe
21
Seite(n)
5895-5904
ISSN
0261-4189
eISSN
1460-2075
Page URI
https://pub.uni-bielefeld.de/record/2577035

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de Vries H, Rüegsegger U, Hübner W, Friedlein A, Langen H, Keller W. Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors. The EMBO journal. 2000;19(21):5895-5904.
de Vries, H., Rüegsegger, U., Hübner, W., Friedlein, A., Langen, H., & Keller, W. (2000). Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors. The EMBO journal, 19(21), 5895-5904. doi:10.1093/emboj/19.21.5895
de Vries, H, Rüegsegger, U, Hübner, Wolfgang, Friedlein, A, Langen, H, and Keller, W. 2000. “Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors”. The EMBO journal 19 (21): 5895-5904.
de Vries, H., Rüegsegger, U., Hübner, W., Friedlein, A., Langen, H., and Keller, W. (2000). Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors. The EMBO journal 19, 5895-5904.
de Vries, H., et al., 2000. Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors. The EMBO journal, 19(21), p 5895-5904.
H. de Vries, et al., “Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors”, The EMBO journal, vol. 19, 2000, pp. 5895-5904.
de Vries, H., Rüegsegger, U., Hübner, W., Friedlein, A., Langen, H., Keller, W.: Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors. The EMBO journal. 19, 5895-5904 (2000).
de Vries, H, Rüegsegger, U, Hübner, Wolfgang, Friedlein, A, Langen, H, and Keller, W. “Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors”. The EMBO journal 19.21 (2000): 5895-5904.

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