Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination

Dichtl B, Blank D, Sadowski M, Hübner W, Weiser S, Keller W (2002)
The EMBO journal 21(15): 4125-4135.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
RNA polymerase II (pol II) transcription termination requires co-transcriptional recognition of a functional polyadenylation signal, but the molecular mechanisms that transduce this signal to pol II remain unclear. We show that Yhh1p/Cft1p, the yeast homologue of the mammalian AAUAAA interacting protein CPSF 160, is an RNA-binding protein and provide evidence that it participates in poly(A) site recognition. Interestingly, RNA binding is mediated by a central domain composed of predicted beta-propeller-forming repeats, which occurs in proteins of diverse cellular functions. We also found that Yhh1p/Cft1p bound specifically to the phosphorylated C-terminal domain (CTD) of pol II in vitro and in a two-hybrid test in vivo. Furthermore, transcriptional run-on analysis demonstrated that yhh1 mutants were defective in transcription termination, suggesting that Yhh1p/Cft1p functions in the coupling of transcription and 3'-end formation. We propose that direct interactions of Yhh1p/Cft1p with both the RNA transcript and the CTD are required to communicate poly(A) site recognition to elongating pol II to initiate transcription termination.
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The EMBO journal
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21
Zeitschriftennummer
15
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4125-4135
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Dichtl B, Blank D, Sadowski M, Hübner W, Weiser S, Keller W. Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination. The EMBO journal. 2002;21(15):4125-4135.
Dichtl, B., Blank, D., Sadowski, M., Hübner, W., Weiser, S., & Keller, W. (2002). Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination. The EMBO journal, 21(15), 4125-4135. doi:10.1093/emboj/cdf390
Dichtl, B., Blank, D., Sadowski, M., Hübner, W., Weiser, S., and Keller, W. (2002). Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination. The EMBO journal 21, 4125-4135.
Dichtl, B., et al., 2002. Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination. The EMBO journal, 21(15), p 4125-4135.
B. Dichtl, et al., “Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination”, The EMBO journal, vol. 21, 2002, pp. 4125-4135.
Dichtl, B., Blank, D., Sadowski, M., Hübner, W., Weiser, S., Keller, W.: Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination. The EMBO journal. 21, 4125-4135 (2002).
Dichtl, Bernhard, Blank, Diana, Sadowski, Martin, Hübner, Wolfgang, Weiser, Stefan, and Keller, Walter. “Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination”. The EMBO journal 21.15 (2002): 4125-4135.

81 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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PMID: 12574128
Functional interactions between the transcription and mRNA 3' end processing machineries mediated by Ssu72 and Sub1.
He X, Khan AU, Cheng H, Pappas DL, Hampsey M, Moore CL., Genes Dev 17(8), 2003
PMID: 12704082
Early formation of mRNP: license for export or quality control?
Jensen TH, Dower K, Libri D, Rosbash M., Mol Cell 11(5), 2003
PMID: 12769839
A role for SSU72 in balancing RNA polymerase II transcription elongation and termination.
Dichtl B, Blank D, Ohnacker M, Friedlein A, Roeder D, Langen H, Keller W., Mol Cell 10(5), 2002
PMID: 12453421
Polyadenylation: a tail of two complexes.
Proudfoot N, O'Sullivan J., Curr Biol 12(24), 2002
PMID: 12498707

44 References

Daten bereitgestellt von Europe PubMed Central.

How RNA polymerase II terminates transcription in higher eukaryotes.
Proudfoot NJ., Trends Biochem. Sci. 14(3), 1989
PMID: 2658217

AUTHOR UNKNOWN, 0
Kin28, the TFIIH-associated carboxy-terminal domain kinase, facilitates the recruitment of mRNA processing machinery to RNA polymerase II.
Rodriguez CR, Cho EJ, Keogh MC, Moore CL, Greenleaf AL, Buratowski S., Mol. Cell. Biol. 20(1), 2000
PMID: 10594013
The ends of the affair: capping and polyadenylation.
Shatkin AJ, Manley JL., Nat. Struct. Biol. 7(10), 2000
PMID: 11017188
The WD repeat: a common architecture for diverse functions.
Smith TF, Gaitatzes C, Saxena K, Neer EJ., Trends Biochem. Sci. 24(5), 1999
PMID: 10322433
A 127 kDa component of a UV-damaged DNA-binding complex, which is defective in some xeroderma pigmentosum group E patients, is homologous to a slime mold protein.
Takao M, Abramic M, Moos M Jr, Otrin VR, Wootton JC, McLenigan M, Levine AS, Protic M., Nucleic Acids Res. 21(17), 1993
PMID: 8371985
Elevated recombination rates in transcriptionally active DNA.
Thomas BJ, Rothstein R., Cell 56(4), 1989
PMID: 2645056
The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools.
Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG., Nucleic Acids Res. 25(24), 1997
PMID: 9396791
Mechanism of poly(A) signal transduction to RNA polymerase II in vitro.
Tran DP, Kim SJ, Park NJ, Jew TM, Martinson HG., Mol. Cell. Biol. 21(21), 2001
PMID: 11585929
Statistical analysis of yeast genomic downstream sequences reveals putative polyadenylation signals.
van Helden J, del Olmo M, Perez-Ortin JE., Nucleic Acids Res. 28(4), 2000
PMID: 10648794
Mammalian poly(A)-binding protein II. Physical properties and binding to polynucleotides.
Wahle E, Lustig A, Jeno P, Maurer P., J. Biol. Chem. 268(4), 1993
PMID: 8428968
The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins.
Yuryev A, Patturajan M, Litingtung Y, Joshi RV, Gentile C, Gebara M, Corden JL., Proc. Natl. Acad. Sci. U.S.A. 93(14), 1996
PMID: 8692929

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