Two phases in the addition of a poly(A) tail.

Sheets, Michael; Wickens, Marvin

doi:10.1101/gad.3.9.1401

Cited by 91 publications

(44 citation statements)

References 44 publications

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“…The two phases of deadenylation observed in this report are reminiscent of the two phases of polyadenylation that occur in the nucleus (Sheets and Wickens 1989). For polyadenylation, the slow addition of the first 10 adenine residues is a kinetically distinct reaction from the subsequent rapid polymerization of the remainder of tail.…”

Section: ~!~I~i I~i I I I I !~I I I I I ! I I I I I I I~ ¸I ! I I I !mentioning

confidence: 70%

3'-UTR-dependent deadenylation by the yeast poly(A) nuclease.

Lowell¹,

Rudner²,

Sachs³

1992

Genes Dev.

129

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Terminal deadenylation rates are also stimulated to different extents by various RNAs. Inversion of the MFA2 3' UTR sequence completely inhibits the terminal deadenylation reaction owing to the presence of an inhibitory element 70 nucleotides from the poly(A) tail. Other sequence elements inserted at a similar distance from the poly(A) tail also interfere with the reaction. These data suggest that the two phases of poly(A) degradation can be regulated by mRNA sequences, and they provide a mechanistic description of how this regulation could occur in vivo.

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Section: ~!~I~i I~i I I I I !~I I I I I ! I I I I I I I~ ¸I ! I I I !mentioning

confidence: 70%

3'-UTR-dependent deadenylation by the yeast poly(A) nuclease.

Lowell¹,

Rudner²,

Sachs³

1992

Genes Dev.

129

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show abstract

“…S1). There are two major restructurings of the CPA that are known to occur during poly(A) tail growth (Humphrey et al 1987;Zarkower and Wickens 1987;Zhang and Cole 1987;Sheets and Wickens 1989;Bardwell and Wickens 1990;Wahle and Kühn 1997). The first occurs when the nascent poly(A) tail is only 10 or so adenosines long, and the initial copy of poly(A) binding protein II (PABII) joins the complex.…”

Section: Discussionmentioning

confidence: 99%

Polyadenylation releases mRNA from RNA polymerase II in a process that is licensed by splicing

Rigo

Martinson²

2009

RNA

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When transcription is coupled to pre-mRNA processing in HeLa nuclear extracts nascent transcripts become attached to RNA polymerase II during assembly of the cleavage/polyadenylation apparatus (CPA), and are not released even after cleavage at the poly(A) site. Here we show that these cleaved transcripts are anchored to the polymerase at their 39 ends by the CPA or, when introns are present, by the larger 39-terminal exon definition complex (EDC), which consists of splicing factors complexed with the CPA. Poly(A) addition releases the RNA from the polymerase when the RNA is anchored only by the CPA. When anchored by the EDC, poly(A) addition remains a requirement, but it triggers release only after being licensed by splicing. The process by which RNA must first be attached to the polymerase by the EDC, and then can only be released following dual inputs from splicing and polyadenylation, provides an obvious opportunity for surveillance as the RNA enters the transport pathway.

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“…Injected RNAs typically are stable, even if they lack poly(A), which simplifies analysis of translational activity. A variety of activation and repression domains have been identified in oocytes (9,10,26,28,33,36,37), and cytoplasmic poly(A) addition and removal events are well documented (30,(38)(39)(40)(41)(42)(43)(44).…”

mentioning

confidence: 99%

Targeted translational regulation using the PUF protein family scaffold

Cooke¹,

Prigge

Opperman³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Regulatory complexes formed on mRNAs control translation, stability, and localization. These complexes possess two activities: one that binds RNA and another-the effector-that elicits a biological function. The Pumilio and FBF (PUF) protein family of RNA binding proteins provides a versatile scaffold to design and select proteins with new specificities. Here, the PUF scaffold is used to target translational activation and repression of specific mRNAs, and to induce specific poly(A) addition and removal. To do so, we linked PUF scaffold proteins to a translational activator, GLD2, or a translational repressor, CAF1. The chimeric proteins activate or repress the targeted mRNAs in Xenopus oocytes, and elicit poly(A) addition or removal. The magnitude of translational control relates directly to the affinity of the RNA-protein complex over a 100-fold range of K d . The chimeric proteins act on both reporter and endogenous mRNAs: an mRNA that normally is deadenylated during oocyte maturation instead receives poly(A) in the presence of an appropriate chimera. The PUF-effector strategy enables the design of proteins that affect translation and stability of specific mRNAs in vivo.CAF1/RNA stability | GLD2/polyadenylation

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Two phases in the addition of a poly(A) tail.

Cited by 91 publications

References 44 publications

3'-UTR-dependent deadenylation by the yeast poly(A) nuclease.

3'-UTR-dependent deadenylation by the yeast poly(A) nuclease.

Polyadenylation releases mRNA from RNA polymerase II in a process that is licensed by splicing

Targeted translational regulation using the PUF protein family scaffold

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