The specific endoribonuclease activity of small nuclear and cytoplasmic α‐RNPs

Konstantinova, Irina D.; Куличкова, В. А.; Evteeva, I. N.; Mittenberg, A. G.; Волкова, Ю. В.; Ermolaeva, J.B.; Gause, L. N.

doi:10.1016/s0014-5793(99)01565-3

Cited by 4 publications

(5 citation statements)

References 24 publications

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“…In addition, it cosedimented with polysomes, but could be released into a more slowly sedimenting RNP fraction following polysome dissociation with EDTA. An endonuclease activity that behaved similarly was identified in RNP complexes from K562 cells (Konstantinova et al 1999).…”

Section: Introductionmentioning

confidence: 76%

An endonuclease activity similar to Xenopus PMR1 catalyzes the degradation of normal and nonsense-containing human β-globin mRNA in erythroid cells

Bremer

Stevens²,

Schoenberg³

2003

RNA

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ABSTRACT␤-globin mRNA bearing a nonsense codon is degraded in the cytoplasm of erythroid cells by endonuclease cleavage, preferentially at UG dinucleotides. An endonuclease activity in polysomes of MEL cells cleaved ␤-globin and albumin mRNA in vitro at many of the same sites as PMR1, an mRNA endonuclease purified from Xenopus liver. Stable transfection of MEL cells expressing normal human ␤-globin mRNA with a plasmid vector expressing the catalytically active form of PMR1 reduced the half-life of ␤-globin mRNA from 12 to 1-2 h without altering GAPDH mRNA decay. The reduced stability of ␤-globin mRNA in these cells was accompanied by an increase in the production of mRNA decay products corresponding to those seen in the degradation of nonsense-containing ␤-globin mRNA. Therefore, ␤-globin mRNA is cleaved in vivo by an endonuclease with properties similar to PMR1. Inhibiting translation with cycloheximide stabilized nonsense-containing ␤-globin mRNA, resulting in a fivefold increase in its steady-state level. Taken together, our results indicate that the surveillance of nonsense-containing ␤-globin mRNA in erythroid cells is a cytoplasmic process that functions on translating mRNA, and endonucleolytic cleavage constitutes one step in the process of ␤-globin mRNA decay.

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Section: Introductionmentioning

confidence: 76%

An endonuclease activity similar to Xenopus PMR1 catalyzes the degradation of normal and nonsense-containing human β-globin mRNA in erythroid cells

Bremer

Stevens²,

Schoenberg³

2003

RNA

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“…This determinant may serve in the recognition of the FR-␣ transcript by a tissue-specific nuclear RNA-degrading machinery. Relatively little is known about the enzymes responsible for the many mRNase activities present in mammalian cells, and attempts are being made to isolate and characterize them (4,10,13,16,26).…”

Section: Discussionmentioning

confidence: 99%

“…The nuclei were separated by centrifugation, resuspended gently in nuclear storage buffer (50 mM Tris [pH 8.3] containing 40% glycerol, 5 mM MgCl 2 , and 0.1 mM EDTA), snap-frozen on dry ice, and stored at Ϫ80°C for up to 4 weeks. For each reaction, 10 7 nuclei were thawed on ice and resuspended in 300 l of reaction buffer (50 mM Tris [pH 8.0], 150 mM KCl, 5 mM MgCl 2 , 0.5 mM MnCl 2 , 2 mM dithiothreitol (DTT), 0.1 mM EDTA, and 10% glycerol) and 60 U of RNase inhibitor from Roche Diagnostic Corp. The reaction was initiated by the addition of ribonucleotides to a final concentration of 0.5 mM ATP, 0.5 mM GTP, 0.5 mM CTP, and 100 Ci of [ 32 P]UTP (800 Ci/mmol) (DuPont-New England Nuclear).…”

mentioning

confidence: 99%

mRNA Instability in the Nucleus Due to a Novel Open Reading Frame Element Is a Major Determinant of the Narrow Tissue Specificity of Folate Receptor α

Zheng

Kelley

Elnakat

et al. 2003

Molecular and Cellular Biology

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“…One unit of PMR1 activity equals the amount of enzyme that completely degrades 7 fmol albumin transcript substrate in 30 min at 22°C (17). more recently a DMSO-inducible endonuclease activity was identified on both nuclear and cytoplasmic mRNPs (26).…”

Section: Estrogen Activates a Global Reorganization Of Translation Inmentioning

confidence: 99%

Polysomal ribonuclease 1 exists in a latent form on polysomes prior to estrogen activation of mRNA decay

Cunningham

Hanson²,

Schoenberg³

2001

Nucleic Acids Research

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Estrogen induces a global change in the translation profile of Xenopus hepatocytes, replacing serum protein synthesis with production of the yolk protein precursor vitellogenin. This is accomplished by the coordinate destabilization of serum protein mRNAs and the transcriptional induction and subsequent stabilization of vitellogenin mRNA. Previous work identified an endonuclease activity whose appearance on polysomes correlated with the disappearance of serum protein mRNAs. This enzyme, polysomal ribonuclease 1 (PMR1), is a novel member of the peroxidase gene family. The current study examined the association of PMR1 with its mRNA targets on polysomes and mRNPs. The highest amount of polysome-bound PMR1 was observed prior to estrogen induction of mRNA decay. Its distribution on sucrose density gradients matched the absorbance profile of polysome-bound mRNA, suggesting that PMR1 forms a latent complex with mRNA. Following dissociation with EDTA the 62 kDa PMR1 sedimented with a larger complex of >670 kDa. Estrogen induces a 22-fold increase in unit enzymatic activity of polysome-bound PMR1, and a time-dependent loss of PMR1 from polysomes in a manner that mirrors the disappearance of albumin mRNA. These data suggest that the key step in the extensive estrogen-induced change in mRNA decay in Xenopus liver is activation of a latent mRNA endonuclease associated with its target mRNA.

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The specific endoribonuclease activity of small nuclear and cytoplasmic α‐RNPs

Cited by 4 publications

References 24 publications

An endonuclease activity similar to Xenopus PMR1 catalyzes the degradation of normal and nonsense-containing human β-globin mRNA in erythroid cells

An endonuclease activity similar to Xenopus PMR1 catalyzes the degradation of normal and nonsense-containing human β-globin mRNA in erythroid cells

mRNA Instability in the Nucleus Due to a Novel Open Reading Frame Element Is a Major Determinant of the Narrow Tissue Specificity of Folate Receptor α

Polysomal ribonuclease 1 exists in a latent form on polysomes prior to estrogen activation of mRNA decay

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