The role of the Brr5/Ysh1 C-terminal domain and its homolog Syc1 in mRNA 3′-end processing in Saccharomyces cerevisiae.

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The role of the Brr5/Ysh1 C-terminal domain and its homolog Syc1 in mRNA 3′-end processing in Saccharomyces cerevisiae. / Nasser, Tommy; Tacahashi, Zhelkovsky A.; He, X.; Sterzer, U.; Jensen, Torben Heick; Dombey, H.; Moore, C.

I: RNA, Bind 12, Nr. 3, 2006, s. 435-45.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Nasser, T, Tacahashi, ZA, He, X, Sterzer, U, Jensen, TH, Dombey, H & Moore, C 2006, 'The role of the Brr5/Ysh1 C-terminal domain and its homolog Syc1 in mRNA 3′-end processing in Saccharomyces cerevisiae.', RNA, bind 12, nr. 3, s. 435-45.

APA

Nasser, T., Tacahashi, Z. A., He, X., Sterzer, U., Jensen, T. H., Dombey, H., & Moore, C. (2006). The role of the Brr5/Ysh1 C-terminal domain and its homolog Syc1 in mRNA 3′-end processing in Saccharomyces cerevisiae. RNA, 12(3), 435-45.

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MLA

Vancouver

Author

Nasser, Tommy ; Tacahashi, Zhelkovsky A. ; He, X. ; Sterzer, U. ; Jensen, Torben Heick ; Dombey, H. ; Moore, C. / The role of the Brr5/Ysh1 C-terminal domain and its homolog Syc1 in mRNA 3′-end processing in Saccharomyces cerevisiae. I: RNA. 2006 ; Bind 12, Nr. 3. s. 435-45.

Bibtex

@article{1feddb30c99a11dbbee902004c4f4f50,
title = "The role of the Brr5/Ysh1 C-terminal domain and its homolog Syc1 in mRNA 3′-end processing in Saccharomyces cerevisiae.",
abstract = "The cleavage/polyadenylation factor (CPF) of Saccharomyces cerevisiae is thought to provide the catalytic activities of the mRNA 3'-end processing machinery, which include endonucleolytic cleavage at the poly(A) site, followed by synthesis of an adenosine polymer onto the new 3'-end by the CPF subunit Pap1. Because of similarity to other nucleases in the metallo-beta-lactamase family, the Brr5/Ysh1 subunit has been proposed to be the endonuclease. The C-terminal domain of Brr5 lies outside of beta-lactamase homology, and its function has not been elucidated. We show here that this region of Brr5 is necessary for cell viability and mRNA 3'-end processing. It is highly homologous to another CPF subunit, Syc1. Syc1 is not essential, but its removal improves the growth of other processing mutants at restrictive temperatures and restores in vitro processing activity to cleavage/ polyadenylation-defective brr5-1 extract. Our findings suggest that Syc1, by mimicking the essential Brr5 C-terminus, serves as a negative regulator of mRNA 3'-end formation.",
author = "Tommy Nasser and Tacahashi, {Zhelkovsky A.} and X. He and U. Sterzer and Jensen, {Torben Heick} and H. Dombey and C. Moore",
note = "Paper id:: 16431986",
year = "2006",
language = "English",
volume = "12",
pages = "435--45",
journal = "RNA",
issn = "1355-8382",
publisher = "Cold Spring Harbor Laboratory Press",
number = "3",

}

RIS

TY - JOUR

T1 - The role of the Brr5/Ysh1 C-terminal domain and its homolog Syc1 in mRNA 3′-end processing in Saccharomyces cerevisiae.

AU - Nasser, Tommy

AU - Tacahashi, Zhelkovsky A.

AU - He, X.

AU - Sterzer, U.

AU - Jensen, Torben Heick

AU - Dombey, H.

AU - Moore, C.

N1 - Paper id:: 16431986

PY - 2006

Y1 - 2006

N2 - The cleavage/polyadenylation factor (CPF) of Saccharomyces cerevisiae is thought to provide the catalytic activities of the mRNA 3'-end processing machinery, which include endonucleolytic cleavage at the poly(A) site, followed by synthesis of an adenosine polymer onto the new 3'-end by the CPF subunit Pap1. Because of similarity to other nucleases in the metallo-beta-lactamase family, the Brr5/Ysh1 subunit has been proposed to be the endonuclease. The C-terminal domain of Brr5 lies outside of beta-lactamase homology, and its function has not been elucidated. We show here that this region of Brr5 is necessary for cell viability and mRNA 3'-end processing. It is highly homologous to another CPF subunit, Syc1. Syc1 is not essential, but its removal improves the growth of other processing mutants at restrictive temperatures and restores in vitro processing activity to cleavage/ polyadenylation-defective brr5-1 extract. Our findings suggest that Syc1, by mimicking the essential Brr5 C-terminus, serves as a negative regulator of mRNA 3'-end formation.

AB - The cleavage/polyadenylation factor (CPF) of Saccharomyces cerevisiae is thought to provide the catalytic activities of the mRNA 3'-end processing machinery, which include endonucleolytic cleavage at the poly(A) site, followed by synthesis of an adenosine polymer onto the new 3'-end by the CPF subunit Pap1. Because of similarity to other nucleases in the metallo-beta-lactamase family, the Brr5/Ysh1 subunit has been proposed to be the endonuclease. The C-terminal domain of Brr5 lies outside of beta-lactamase homology, and its function has not been elucidated. We show here that this region of Brr5 is necessary for cell viability and mRNA 3'-end processing. It is highly homologous to another CPF subunit, Syc1. Syc1 is not essential, but its removal improves the growth of other processing mutants at restrictive temperatures and restores in vitro processing activity to cleavage/ polyadenylation-defective brr5-1 extract. Our findings suggest that Syc1, by mimicking the essential Brr5 C-terminus, serves as a negative regulator of mRNA 3'-end formation.

M3 - Journal article

VL - 12

SP - 435

EP - 445

JO - RNA

JF - RNA

SN - 1355-8382

IS - 3

ER -