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Role of cleavage and polyadenylation specificity factor 100: anchoring poly(A) sites and modulating transcription termination
Author(s) -
Lin Juncheng,
Xu Ruqiang,
Wu Xiaohui,
Shen Yingjia,
Li Qingshun Q.
Publication year - 2017
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.13611
Subject(s) - cleavage and polyadenylation specificity factor , polyadenylation , biology , microbiology and biotechnology , terminator (solar) , rna polymerase ii , transcription factor , gene silencing , transcription (linguistics) , rna binding protein , gene , genetics , rna , gene expression , promoter , linguistics , philosophy , ionosphere , physics , astronomy
Summary CPSF 100 is a core component of the cleavage and polyadenylation specificity factor ( CPSF ) complex for 3′‐end formation of mRNA , but it still has no clear functional assignment. CPSF 100 was reported to play a role in RNA silencing and promote flowering in Arabidopsis. However, the molecular mechanisms underlying these phenomena are not fully understood. Our genetics analyses indicate that plants with a hypomorphic mutant of CPSF 100 ( esp5 ) show defects in embryogenesis, reduced seed production or altered root morphology. To unravel this puzzle, we employed a poly(A) tag sequencing protocol and uncovered a different poly(A) profile in esp5 . This transcriptome‐wide analysis revealed alternative polyadenylation of thousands of genes, most of which result in transcriptional read‐through in protein‐coding genes. At CPSF 100 also affects poly(A) signal recognition on the far‐upstream elements; in particular it prefers less U‐rich sequences. Importantly, At CPSF 100 was found to exert its functions through the change of poly(A) sites on genes encoding binding proteins, such as nucleotide‐binding, RNA ‐binding and poly(U)‐binding proteins. In addition, through its interaction with RNA Polymerase II C‐terminal domain ( CTD ) and affecting the expression level of CTD phosphatase‐like 3 ( CPL 3 ), At CPSF 100 is shown to potentially ensure transcriptional termination by dephosphorylation of Ser2 on the CTD . These data suggest a key role for CPSF 100 in locating poly(A) sites and affecting transcription termination.

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