Polynucleotide phosphorylase is a component of a novel plant poly(A) polymerase.

The Journal of Biological Chemistry
Q S LiArthur G Hunt

Abstract

We have isolated cDNA clones encoding a novel RNA-binding protein that is a component of a multisubunit poly(A) polymerase from pea seedlings. The encoded protein bears a significant resemblance to polynucleotide phosphorylases (PNPases) from bacteria and chloroplasts. More significantly, this RNA-binding protein is able to degrade RNAs with the resultant production of nucleotide diphosphates, and it can add extended polyadenylate tracts to RNAs using ADP as a donor for adenylate moieties. These activities are characteristic of PNPase. Antibodies raised against the cloned protein simultaneously immunoprecipitate both poly(A) polymerase and PNPase activity. We conclude from these studies that PNPase is the RNA-binding cofactor for this poly(A) polymerase and is an integral player in the reaction catalyzed by this enzyme. The identification of this RNA-binding protein as PNPase, which is a chloroplast-localized enzyme known to be involved in mRNA 3'-end determination and turnover (Hayes, R., Kudla, J., Schuster, G., Gabay, L., Maliga, P., and Gruissem, W. (1996) EMBO J. 15, 1132-1141), raises interesting questions regarding the subcellular location of the poly(A) polymerase under study. We have reexamined this issue, and we find ...Continue Reading

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Citations

Jun 29, 2000·Biochemical and Biophysical Research Communications·A G HuntB D Mogen
Feb 27, 2001·Nucleic Acids Research·Y Zuo, M P Deutscher
Oct 18, 2002·Nucleic Acids Research·Sacha Baginsky, Wilhelm Gruissem
Sep 12, 2000·Journal of Virology·J Jin, L A Guarino
Sep 13, 2006·Molecular and Cellular Biology·Hsiao-Wen ChenSamuel W French
Feb 27, 2008·The Plant Journal : for Cell and Molecular Biology·Denghui XingQingshun Quinn Li
Jun 17, 1999·FEMS Microbiology Reviews·R Rauhut, G Klug
Mar 9, 2018·Nucleic Acids Research·Marina ToompuuHoward T Jacobs

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