Nuclear exoribonucleases. III. Isolation and properties of the enzyme from normal and malignant tissues of the mouse

Sporn, Michael B.; Lazarus, Harrison M.; Smith, Joseph M.; Henderson, William R.

doi:10.1021/bi00832a053

Cited by 59 publications

(19 citation statements)

References 42 publications

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“…This 40,000 Mr enzyme, which we designate 2'-phosphodiesterase-interferon (2'-PDi), differs from snake venom phosphodiesterase (31) and from a phosphodiesterase observed in leukemia cells (32). The latter enzyme prefers substrates with a 5' phosphate and degrades tRNA processively beyond its C-C-A end (33).…”

Section: Methodsmentioning

confidence: 99%

An interferon-induced phosphodiesterase degrading (2'-5') oligoisoadenylate and the C-C-A terminus of tRNA.

Schmidt¹,

Chernajovsky²,

Shulman³

et al. 1979

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

181

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Section: Methodsmentioning

confidence: 99%

An interferon-induced phosphodiesterase degrading (2'-5') oligoisoadenylate and the C-C-A terminus of tRNA.

Schmidt¹,

Chernajovsky²,

Shulman³

et al. 1979

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

181

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“…Reaction conditions for both the ascites exoribonuclease hydrolysis (32) and polynucleotide phosphorylase phosphorolysis (40) En2ymes. Exoribonuclease specific for 3'-OH termini was isolated from the nuclei of Ehrlich ascites tumor cells and characterized as described (38). Polynucleotide phosphorylase (no.…”

Section: Methodsmentioning

confidence: 99%

Polyriboadenylate Sequences at the 3′-Termini of Ribonucleic Acid Obtained from Mammalian Leukemia and Sarcoma Viruses

Phillips

Park

Hollis

1974

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

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The location of poly(A) sequences in the RNA of mammalian RNA-tumor viruses was determined by enzymatic analyses. The 56-64S viral genomic RNAs, the 20-40S viral subunit RNAs, and the 4-5S poly(A) sequences excised from these viral RNAs were subjected to either hydrolysis with a 3'-OH specific exoribonuclease from Ehrlich ascites tumor cells or phosphorolysis from the 3'-termini with polynucleotide phosphorylase from Micrococcus luteus. Purified adenosine-labeled poly(A) fragments, excised from genomic viral RNAs by RNase A and T1 digestion, were hydrolyzed with the 3'-OH specific exoribonuclease for various periods of time. Poly(U) filter binding studies of the residual poly(A) indicated that 97% of the poly(A) fragments were hydrolyzed. Adenosinelabeled genomic and subunit viral RNAs and excised poly(A) fragments were phosphorolyzed from their 3'-termini for various periods of time with polynucleotide phosphorylase. The degree of phosphorolysis was monitored by poly(U) filter binding studies, and CC1,COOH insolubility and solubility determinations. There was an initial preferential rate of phosphorolysis of the poly(A) sequences of genomic and subunit viral RNAs as compared to the total adenosine-labeled viral RNAs. The data from these two different enzymatic mechanisms of action indicated conclusively that the poly(A) sequences were located at the 3'-termini of genomic and subunit viral RNAs.

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“…The precursors used for the syi nRNA are supplied from the cytoplasrr free nucleotides and from the degradati turning-over hnRNA and/or pre-rRNA Previous studies on uridine metal cultured cells (reviewed by Hauschka, I shown that UTP arises from both synthe and the phosphorylation of UMP derive degradation of RNA molecules within ti nucleotides to be re-utilized, they have 5'-phosphorylated form. The existenc nuclear and cytoplasmic enzymes wi nuclease activity in animal cells has bee (Harris, 1963;Sporn et al, 1969;Kum, 1979).…”

Section: Calculationsmentioning

confidence: 99%

Re-utilization of pyrimidine nucleotides during rat liver regeneration

Nikolov¹,

Dabeva²

1985

Biochemical Journal

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The changes in the specific radioactivities of the pool of total acid-soluble uridine nucleotides and of uridine and cytidine components of total cellular and nuclear RNA were monitored in regenerating rat liver for 12 days after partial hepatectomy. Evidence is presented for the re-utilization of pyrimidine nucleotides derived from cytoplasmic RNA degradation for the synthesis of new RNA. The extent of recycling was assessed and the true rate of rRNA turnover determined more accurately. The reutilization of the uridine components of RNA was 7.0%/day during the proliferative and 3.2%/day during the post-proliferative phase, whereas that of the cytidine nucleotides was more pronounced (9.6%/day and 18.1%/day respectively). The results reveal the existence of partial compartmentalization of pyrimidine ribonucleoside triphosphate pools in the nucleus and cytoplasm of rat liver cells.

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Nuclear exoribonucleases. III. Isolation and properties of the enzyme from normal and malignant tissues of the mouse

Cited by 59 publications

References 42 publications

An interferon-induced phosphodiesterase degrading (2'-5') oligoisoadenylate and the C-C-A terminus of tRNA.

An interferon-induced phosphodiesterase degrading (2'-5') oligoisoadenylate and the C-C-A terminus of tRNA.

Polyriboadenylate Sequences at the 3′-Termini of Ribonucleic Acid Obtained from Mammalian Leukemia and Sarcoma Viruses

Re-utilization of pyrimidine nucleotides during rat liver regeneration

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