2′,5′-phosphodiesterase activity depends upon the presence of a 3′-hydroxyl moiety in the penultimate position of the oligonucleotide substrate

Alster, D.; Brózda, Danuta; Kitade, Yukio; Wong, Alice; Charubala, Ramamurthy; Pfleiderer, Wolfgang; Torrence, Paul F.

doi:10.1016/s0006-291x(86)80209-1

Cited by 11 publications

(6 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The results obtained herein are in agreement with our earlier findings [4] that substitution by TIME hntnutes) Pig. 1.…”

Section: Resultssupporting

confidence: 93%

“…Recently, we reported [4] that degradation by the 2' ,5'-phosphodiesterase activity requires a 3 ' -hydroxyl group on the penultimate nucleotide unit of the 2 ' ,5 ' -oligonucleotide. Specifically we demonstrated that the 3 ' -deoxyadenosine substituted 2-5A analog, pS'A2'p5'(3'dA)-2'pS'A, possessed the same high degree of resistance to degradation by the 2' ,5 ' -phosphodiesterase activity as did p5 ' (3 ' dA)2 ' p5 ' (3 ' dA)-2'p5'(3'dA) shown [5,6] to be resistant.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Degradation by the 2',5'‐phosphodiesterase activity of mouse cells requires the presence of a ribo hydroxyl group in the penultimate position of the oligonucleotide substrate

et al. 1987

Self Cite

View full text Add to dashboard Cite

A series of 9‐β‐D‐xylofuranosyladenine (xyloA or xyloadenosine) substituted analogs of 2‐5A core trimer and tetramer were examined for their ability to be degraded by the 2',5'‐phosphodiesterase activity of cytoplasmic extracts of mouse L cells. Two distinct groups of xyloA‐substituted analogs could be readily discriminated. The first group contained xyloadenosine at the 2'‐termini and included A2'p5'A2'p5'(xyloA) and A2'p5'A2/p5'A2'p5'(xyloA). These oligomers behaved as did their parent oligoadenylates in that they were equally sensitive to degradation by the 2',5'‐phosphodiesterase activity. The second group of oligonucleotides bore a xyloadenosine residue in the penultimate nucleotide residues of the oligomers and included A2'p5'(xyloA)2'p5'(xyloA), (xyloA)2'p5'(xyloA)2'p5'(xyloA), A2'p5'A2'p5'(xyloA)2'p5'(xyloA) and (xyloA)2'p5' (xyloA)2'p5'(xyloA)2'p5'(xyloA). This group was quite resistant to 2',5'‐phosphodiesterase activity. In all, the findings demonstrate that the ribo configuration 3'‐hydroxyl group in the penultimate nucleotide of the oligonucleotide substrate is a prerequisite for the 2',5'‐phosphodiesterase activity.

show abstract

“…The results obtained herein are in agreement with our earlier findings [4] that substitution by TIME hntnutes) Pig. 1.…”

Section: Resultssupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Degradation by the 2',5'‐phosphodiesterase activity of mouse cells requires the presence of a ribo hydroxyl group in the penultimate position of the oligonucleotide substrate

et al. 1987

Self Cite

View full text Add to dashboard Cite

show abstract

“…One such modification mentioned earlier is that of the complete 3'-O-methylation of 2'5' (A), which produces a derivative unable to activate RNase L in vitro, but which is even more active than 2'5' (A), itself when only the 2' terminal ribose is 3'-0methylated. It has also been shown that sensitivity to the action of z',5'phosphodiesterase in mouse L cell extracts requires the presence of the 3' hydroxyl group of the penultimate nucleotide of the z's'(A), 5'-monophosphate (Alster et al, 1986) Blockage of this 3' hydroxyl group of the z '~' ( A )~ may therefore be a means of increasing their resistance to enzymatic degradation both extracellularly and intracellularly. Whether a similar or other modification(s) to Ap& increases its resistance to enzymatic degradation is not known.…”

Section: (9) Further Aspects In the Design Of Adenosine Analoguesmentioning

confidence: 99%

Ribonucleotide Metabolism ‐ Fresh Approaches to Viral and Cancer Chemotherapy*

Alderson

1989

Biological Reviews

View full text Add to dashboard Cite

“…It has been shown that sensitivity to the action of z',5'phosphodiesterase in mouse L-cell extracts requires the presence of the 3'-hydroxyl group of the penultimate nucleotide of the z's'(A), 5'-monophosphate (Alster et al, 1986). It has been shown that sensitivity to the action of z',5'phosphodiesterase in mouse L-cell extracts requires the presence of the 3'-hydroxyl group of the penultimate nucleotide of the z's'(A), 5'-monophosphate (Alster et al, 1986).…”

mentioning

confidence: 99%

“…One such modification is the blocking of the 3' position of the ribose, which should still allow the adenosine analogue to be utilized for the synthesis of both types of oligoribonucleotide metabolites. It has been shown that sensitivity to the action of z',5'phosphodiesterase in mouse L-cell extracts requires the presence of the 3'-hydroxyl group of the penultimate nucleotide of the z's'(A), 5'-monophosphate (Alster et al, 1986). Blockage of this 3'-hydroxyl group of the ~' S ' ( A )~ may therefore be a means of increasing the resistance of at least some of the oligomers formed from intracellular degradation.…”

mentioning

confidence: 99%

New Targets for Cancer Chemotherapy – Poly(adpribosylation) Processing and Polyisoprene Metabolism*

Alderson

1990

Biological Reviews

View full text Add to dashboard Cite

CONTENTS* This paper is dedicated to the memory of my late wife, Dr Elena Popova. 23-2 624T. ALDERSON proteins. T h e modification may be with a single ADP-ribose moiety, termed mono(ADP-ribosylation), or with longer chains (linear or branched) of covalently linked ADP-ribose residues, termed poly(ADP-ribosylation). T h e majority of mono(ADP-ribosylated) conjugates are localized outside the nucleus, and they are generally much more abundant than poly(ADP-ribosylated) conjugates.T h e nuclear proteins known to be poly(ADP-ribosylated) by A D P R T are histones ( H I , Hza, Hzb, H3, and H5), non-histones [lamins and high mobility group proteins (HMG)] and various D N A enzymes, namely, D N A ligase 11, DNA polymerase a , D N A polynierase p, deoxynucleotidyl terminal transferase, Ca2'/Mg2+-dependent endonuclease, D N A topoisomerase I , and A D P R T itself. T h e apparent regulatory roles of the poly(ADP-ribosylation) modification of histones and the D N A replication and repair enzymes have been previously discussed (Alderson, I 989).Poly(ADP-ribosylation) exhibits a cell-cycle oscillation with a maximum coinciding with S phase after a release of GI block; its removal appears to be carried out by the co-operative action of poly(ADP-ribose) glycohydrolase and ADP-ribosyl protein lyase.Most of the functions of the poly(ADP-ribosylation) modification process have been attributed to the fact that A D P R T has an absolute requirement for DNA for its activity.

show abstract

2′,5′-phosphodiesterase activity depends upon the presence of a 3′-hydroxyl moiety in the penultimate position of the oligonucleotide substrate

Cited by 11 publications

References 14 publications

Degradation by the 2',5'‐phosphodiesterase activity of mouse cells requires the presence of a ribo hydroxyl group in the penultimate position of the oligonucleotide substrate

Degradation by the 2',5'‐phosphodiesterase activity of mouse cells requires the presence of a ribo hydroxyl group in the penultimate position of the oligonucleotide substrate

Ribonucleotide Metabolism ‐ Fresh Approaches to Viral and Cancer Chemotherapy*

New Targets for Cancer Chemotherapy – Poly(adpribosylation) Processing and Polyisoprene Metabolism*

Contact Info

Product

Resources

About