Maturation-specific deadenylation in Xenopus oocytes requires nuclear and cytoplasmic factors

Varnum, Susan M.; Hurney, Carol A.; Wormington, W M

doi:10.1016/0012-1606(92)90113-u

Cited by 40 publications

(25 citation statements)

References 36 publications

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“…The ACE-binding translational repressor could thus target a deadenylase to tPA mRNA, or itself have deadenylase activity. In Xenopus oocytes, a nuclear deadenylase released after GVBD is implicated in the default deadenylation of mRNAs lacking CPEs (Varnum et al 1992;Wormington et al 1996). In mouse oocytes, such a default deadenylation was not prevented by the ACE competitor, suggesting that the default process is different from that involved in the specific deadenylation of tPA mRNA.…”

Section: Discussionmentioning

confidence: 93%

Masking, unmasking, and regulated polyadenylation cooperate in the translational control of a dormant mRNA in mouse oocytes

Stutz¹,

Conne²,

Huarte³

et al. 1998

Genes Dev.

106

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The mechanisms responsible for translational silencing of certain mRNAs in growing oocytes, and for their awakening during meiotic maturation, are not completely elucidated. We show that binding of a ∼80-kD protein to a UA-rich element in the 3 UTR of tissue-type plasminogen activator mRNA, a mouse oocyte mRNA that is translated during meiotic maturation, silences the mRNA in primary oocytes. Translation can be triggered by injecting a competitor transcript that displaces this silencing factor, without elongation of a pre-existing short poly(A) tail, the presence of which is mandatory. During meiotic maturation, cytoplasmic polyadenylation is necessary to maintain a poly(A) tail, but the determining event for translational activation appears to be the modification or displacement of the silencing factor.

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Section: Discussionmentioning

confidence: 93%

Masking, unmasking, and regulated polyadenylation cooperate in the translational control of a dormant mRNA in mouse oocytes

Stutz¹,

Conne²,

Huarte³

et al. 1998

Genes Dev.

106

View full text Add to dashboard Cite

show abstract

“…been reported to be inactive in deadenylation unless they are further purified (17,52). Interestingly, it has been reported that PARN isolated from Xenopus oocytes co-purifies with two polypeptides being 74 and 62 kDa in sizes, the latter most likely being a proteolytic product that lacks the C terminus of the former (19,52).…”

Section: Discussionmentioning

confidence: 99%

Inhibition of mRNA Deadenylation by the Nuclear Cap Binding Complex (CBC)

Balatsos

Nilsson

Mazza

et al. 2006

Journal of Biological Chemistry

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Poly(A)-specific ribonuclease (PARN) is a cap-interacting and poly(A)-specific 3-exoribonuclease. Here we have investigated how the cap binding complex (CBC) affects human PARN activity. We showed that CBC, via its 80-kDa subunit (CBP80), inhibited PARN, suggesting that CBC can regulate mRNA deadenylation. The CBCmediated inhibition of PARN was cap-independent, and in keeping with this, the CBP80 subunit alone inhibited PARN. Our data suggested a new function for CBC, identified CBC as a potential regulator of PARN, and emphasized the importance of communication between the two extreme ends of the mRNA as a key strategy to regulate mRNA degradation. Based on our data, we have proposed a model for CBC-mediated regulation of PARN, which relies on an interaction between CBP80 and PARN. Association of CBC with PARN might have importance in the regulated recruitment of PARN to the nonsense-mediated decay pathway during the pioneer round of translation.

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“…Human PARN was originally identified as a 74 kDa enzyme [6], but a proteolytic 54 kDa fragment has also been purified [7]. PARN isolated from Xenopus oocytes co-purifies with two polypeptides being 74 and 62 kDa in sizes, the latter most likely being a proteolytic product that lacks the C-terminus of the former [8,9]. The important properties of PARN are its high specificity for single-stranded poly(A) and a requirement for a 3 0 hydroxyl group for activity [6,10].…”

Section: Introductionmentioning

confidence: 99%

Inhibition of human poly(A)-specific ribonuclease (PARN) by purine nucleotides: kinetic analysis

Balatsos

Anastasakis

Stathopoulos

2009

Journal of Enzyme Inhibition and Medicinal Chemistry

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Poly(A)-specific ribonuclease (PARN) is a cap-interacting and poly(A)-specific 30 -exoribonuclease that efficiently degrades mRNA poly(A) tails. Based on the enzyme's preference for its natural substrates, we examined the role of purine nucleotides as potent effectors of human PARN activity. We found that all purine nucleotides tested can reduce poly(A) degradation by PARN. Detailed kinetic analysis revealed that RTP nucleotides behave as non-competitive inhibitors while RDP and RMP exhibit competitive inhibition. Mg 2 þ which is a catalytically important mediator of PARN activity can release inhibition of RTP and RDP but not RMP. Although many strategies have been proposed for the regulation of PARN activity, very little is known about the modulation of PARN activity by small molecule effectors, such as nucleotides. Our data imply that PARN activity can be modulated by purine nucleotides in vitro, providing an additional simple regulatory mechanism.

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Maturation-specific deadenylation in Xenopus oocytes requires nuclear and cytoplasmic factors

Cited by 40 publications

References 36 publications

Masking, unmasking, and regulated polyadenylation cooperate in the translational control of a dormant mRNA in mouse oocytes

Masking, unmasking, and regulated polyadenylation cooperate in the translational control of a dormant mRNA in mouse oocytes

Inhibition of mRNA Deadenylation by the Nuclear Cap Binding Complex (CBC)

Inhibition of human poly(A)-specific ribonuclease (PARN) by purine nucleotides: kinetic analysis

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