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Gene Review:

YTH1 - Yth1p

Saccharomyces cerevisiae S288c

Synonyms: YPR107C, Yeast 30 kDa homolog 1, mRNA 3'-end-processing protein YTH1

Barabino, S.M. et al., Tacahashi, Y. et al., Birse, C.E. et al., Barabino, S.M. et al.

Barabino, Ohnacker, Keller,

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High impact information on YTH1

In contrast, the mutation of factors involved in the subsequent polyadenylation step (PAP1, FIP1, and YTH1) had little effect [1].
Finally, we find that Yth1p binds to CYC1 pre-mRNA in the vicinity of the cleavage site [2].
Distinct roles of two Yth1p domains in 3'-end cleavage and polyadenylation of yeast pre-mRNAs [2].
A single point mutation in the highly conserved second zinc finger impairs both cleavage and polyadenylation, and affects the ability of Yth1p to interact with the pre-mRNA and other CPF subunits [2].
Here, we demonstrate that Yth1p is also required for the cleavage reaction and that two protein domains have distinct roles in 3'-end processing [2].

Biological context of YTH1

Yth1, a subunit of yeast Cleavage Polyadenylation Factor (CPF), contains five CCCH zinc fingers [3].

Physical interactions of YTH1

We demonstrate that Yth1p is a component of PF I that interacts in vivo and in vitro with Fip1p, a known PF I subunit [4].

Analytical, diagnostic and therapeutic context of YTH1

Functional dissection of the zinc finger and flanking domains of the Yth1 cleavage/polyadenylation factor [3].

References

Coupling termination of transcription to messenger RNA maturation in yeast. Birse, C.E., Minvielle-Sebastia, L., Lee, B.A., Keller, W., Proudfoot, N.J. Science (1998) [Pubmed]
Distinct roles of two Yth1p domains in 3'-end cleavage and polyadenylation of yeast pre-mRNAs. Barabino, S.M., Ohnacker, M., Keller, W. EMBO J. (2000) [Pubmed]
Functional dissection of the zinc finger and flanking domains of the Yth1 cleavage/polyadenylation factor. Tacahashi, Y., Helmling, S., Moore, C.L. Nucleic Acids Res. (2003) [Pubmed]
The 30-kD subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are RNA-binding zinc finger proteins. Barabino, S.M., Hübner, W., Jenny, A., Minvielle-Sebastia, L., Keller, W. Genes Dev. (1997) [Pubmed]

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AGOS_AEL331W	Ashbya gossypii ATCC 10895
KLLA0F08129g	Kluyveromyces lactis NRRL Y-1140
MGG_00680	Magnaporthe oryzae 70-15
NCU08353	Neurospora crassa OR74A
yth1	Schizosaccharomyces pombe 972h-

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